EzCatDB: S00021

DB codeS00021
RLCP classification1.30.300.2
CATH domainDomain 11.10.530.40Catalytic domain
E.C.3.2.1.17
CSA206l

CATH domainRelated DB codes (homologues)
1.10.530.40S00265

Enzyme Name
Swiss-protKEGG

P00720
Protein nameLysozymelysozyme
muramidase
globulin G
mucopeptide glucohydrolase
globulin G1
N,O-diacetylmuramidase
lysozyme g
L-7001
1,4-N-acetylmuramidase
mucopeptide N-acetylmuramoylhydrolase
PR1-lysozyme
SynonymsEC 3.2.1.17
Lysis protein
Muramidase
Endolysin


Swiss-prot:Accession NumberP00720
Entry nameLYS_BPT4
ActivityHydrolysis of (1->4)-beta-linkages between N- acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Subunit
Subcellular location
Cofactor


SubstratesProductsintermediates
KEGG-idC00851C00889C00001C00851C04394C00140
CompoundChitodextrinPeptidoglycanH2OChitodextrinPeptidoglycan(N-acetyl-D-glucosamine)N-Acetyl-D-glucosamine
Typeamide group,polysaccharideamino acids,amide group,amine group,carbohydrate,peptide/protein,polysaccharideH2Oamide group,polysaccharideamino acids,amide group,amine group,carbohydrate,lipid,peptide/protein,polysaccharideamide group,carbohydrate
102lAUnboundUnbound
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147lAUnboundUnbound
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148lEUnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:NAG-AMU-ALA-GLU-API-ALA(chain S:covalent bond with mutated residue Glu26)
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Active-site residues
resource
Swiss-prot;LYCV_BPT4;P00720
pdbCatalytic residuescomment
102lAGLU 11;ASP 20
mutant C54T, C97A, insertion N40-A
103lAGLU 11;ASP 20
mutant C54T, C97A, insertion N40-SLD
104lAGLU 11;ASP 20
mutant C54T, C97A, insertion S44-AA
104lBGLU 11;ASP 20
mutant C54T, C97A, insertion S44-AA
107lAGLU 11;ASP 20
mutant S44G, C54T, C97A
108lAGLU 11;ASP 20
mutant S44I, C54T, C97A
109lAGLU 11;ASP 20
mutant S44K, C54T, C97A
110lAGLU 11;ASP 20
mutant S44L, C54T, C97A
111lAGLU 11;ASP 20
mutant S44N, C54T, C97A
112lAGLU 11;ASP 20
mutant S44P, C54T, C97A
113lAGLU 11;ASP 20
mutant S44R, C54T, C97A
114lAGLU 11;ASP 20
mutant S44T, C54T, C97A
115lAGLU 11;ASP 20
mutant S44V, C54T, C97A
116lAGLU 11;ASP 20
mutant S44W, C54T, C97A
116lBGLU 11;ASP 20
mutant S44W, C54T, C97A
116lCGLU 11;ASP 20
mutant S44W, C54T, C97A
116lDGLU 11;ASP 20
mutant S44W, C54T, C97A
118lAGLU 11;ASP 20
mutant C54T, C97A, A130S
119lAGLU 11;ASP 20
mutant C54T, C97A, A134S
120lAGLU 11;ASP 20
mutant A41S, C54T, C97A
122lAGLU 11;ASP 20
mutant C54T, A73S, C97A
123lAGLU 11;ASP 20
mutant C54T, A82S, C97A
125lAGLU 11;ASP 20
mutant C54T, C97A, A98S
126lAGLU 11;ASP 20
mutant C54T, C97A, V149T
127lAGLU 11;ASP 20
mutant C54T, V75T, C97A
128lAGLU 11;ASP 20
mutant C54T, V87T, C97A
129lAGLU 11;ASP 20
mutant C54T, A93T, C97A
130lAGLU 11;ASP 20
mutant C54T, C97A, T151S
131lAGLU 11;ASP 20
mutant T26S, C54T, C97A
137lAGLU 11;ASP 20
mutant S44F, C54T, C97A
137lBGLU 11;ASP 20
mutant S44F, C54T, C97A
138lAGLU 11;ASP 20
mutant C54T, A93C, C97A
139lAGLU 11;ASP 20
mutant C54T, N68C, A93C, C97A
140lAGLU 11;ASP 20
mutant C54T, C97A, L121A, A129M, F153L
141lAGLU 11;ASP 20
mutant C54T, C97A, L121A, A129M, V149I
142lAGLU 11;ASP 20
mutant C54T, C97A, L121A, A129V, L133A, F153L
143lAGLU 11;ASP 20
mutant C54T, C97A, L121A, A129V, L133M, F153L
144lAGLU 11;ASP 20
mutant C54T, C97A, L121I, A129L, L133M, F153W
145lAGLU 11;ASP 20
mutant C54T, C97A, L121I, A129W, L133M
146lAGLU 11;ASP 20
mutant C54T, C97A, L121M, A129L, L133M, V149I, F153W
147lAGLU 11;ASP 20
mutant C54T, C97A, L121M, L133V, F153L
148lEGLU 11;ASP 20
mutant T26E, C54T, C97A
149lAGLU 11;ASP 20
mutant I3L
150lAGLU 11;ASP 20
mutant M6I
150lBGLU 11;ASP 20
mutant M6I
150lCGLU 11;ASP 20
mutant M6I
150lDGLU 11;ASP 20
mutant M6I
151lAGLU 11;ASP 20
mutant T34A, K35A, S36A, P37A
152lAGLU 11;ASP 20
mutant I3C, I9C, T21C, C54T, T142C, L164C
155lAGLU 11;ASP 20
mutant C54T, C97A, T115A, S117A
156lAGLU 11;ASP 20
mutant C54T, A97A, T115A, R119A
157lAGLU 11;ASP 20
mutant C54T, C97A, T115A, N116A, S117A, R119A, M120A, Q122A, Q123A
158lAGLU 11;ASP 20
mutant C54T, C97A, S117A, R119A
159lAGLU 11;ASP 20
mutant C54T, C97A, R119A, Q123A
160lAGLU 11;ASP 20
mutant C54T, C97A, M120A
161lAGLU 11;ASP 20
mutant C54T, C97A, N116A
162lAGLU 11;ASP 20
mutant C54T, C97A, Q122A
163lAGLU 11;ASP 20
mutant C54T, C97A, Q123A
164lAGLU 11;ASP 20
mutant C54T, C97A, R119A
165lAGLU 11;ASP 20
mutant C54T, C97A, S117A
166lAGLU 11;ASP 20
mutant C54T, C97A, T115A
167lAGLU 11;ASP 20
mutant I3C, I9C, C54T, L164C
167lBGLU 11;ASP 20
mutant I3C, I9C, C54T, L164C
168lAGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A
168lBGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A
168lCGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A
168lDGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A
168lEGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A
169lAGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A, Y139A, N140A, Q141A
169lBGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A, Y139A, N140A, Q141A
169lCGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A, Y139A, N140A, Q141A
169lDGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A, Y139A, N140A, Q141A
169lEGLU 11;ASP 20
mutant E128A, V131A, N132A, K135A, S136A, R137A, Y139A, N140A, Q141A
170lAGLU 11;ASP 20
mutant C54S, C97S, A146C
171lAGLU 11;ASP 20
mutant E45A, C54T, C97A
172lAGLU 11;ASP 20
mutant I3C
173lAGLU 11;ASP 20
mutant K16E, R119E, K135E, K147E
174lAGLU 11;ASP 20
mutant T34A, K35A, S36A, P37A, S38D, N40A, S44A, E45A, D47A, K48A, C54T, T97A
174lBGLU 11;ASP 20
mutant T34A, K35A, S36A, P37A, S38D, N40A, S44A, E45A, D47A, K48A, C54T, T97A
175lAGLU 11;ASP 20
mutant C54T, R96A, C97A
175lBGLU 11;ASP 20
mutant C54T, R96A, C97A
176lAGLU 11;ASP 20
mutant L32T, T34K, K35V, S36D, P37G, S38N, L39S, C54T, C97A
176lBGLU 11;ASP 20
mutant L32T, T34K, K35V, S36D, P37G, S38N, L39S, C54T, C97A
177lAGLU 11;ASP 20
mutant C54T, C97A, D127C, R154C
178lAGLU 11;ASP 20
mutant C54T, C97A, D127C, R154C
179lAGLU 11;ASP 20
mutant C54A, C97A, D127C, R154C
180lAGLU 11;ASP 20
mutant T26E, C54T, C97A
180lBGLU 11;ASP 20
mutant T26E, C54T, C97A
181lAGLU 11;ASP 20
mutant C54T, C97A, L99A
182lAGLU 11;ASP 20
mutant C54T, C97A, L99A
183lAGLU 11;ASP 20
mutant C54T, C97A, L99A
184lAGLU 11;ASP 20
mutant C54T, C97A, L99A
185lAGLU 11;ASP 20
mutant C54T, C97A, L99A
186lAGLU 11;ASP 20
mutant C54T, C97A, L99A
187lAGLU 11;ASP 20
mutant C54T, C97A, L99A
188lAGLU 11;ASP 20
mutant C54T, C97A, L99A
189lAGLU 11;ASP 20
mutant I3L, S38D, A41V, A82P, N116D, V131A, N144D
190lAGLU 11;ASP 20
mutant N53A, N55A, V57A
191lAGLU 11;ASP 20
mutant N53A, N55A, V57A, E128A, V131A, N132A
192lAGLU 11;ASP 20
mutant N40A, S44A, E45A, D47A, K48A, C54T, C97A, D127A, E128A, V131A, N132A
195lAGLU 11;ASP 20
mutant C54T, C97A, A129L
196lAGLU 11;ASP 20
mutant C54T, C97A, A129M
197lAGLU 11;ASP 20
mutant C54T, C97A, A129M, F153A
198lAGLU 11;ASP 20
mutant C54T, C97A, L121A, A129L
199lAGLU 11;ASP 20
mutant C54T, C97A, L121A, A129M
1b6iAGLU 11;ASP 20
mutant C54T, C97A, T21C, K124C
1c60AGLU 11;ASP 20
mutant C54T, C97A, F153A
1c61AGLU 11;ASP 20
mutant C54T, C97A, F153A
1c62AGLU 11;ASP 20
mutant C54T, C97A, F153A
1c63AGLU 11;ASP 20
mutant C54T, C97A, L121A
1c64AGLU 11;ASP 20
mutant C54T, C97A, L121A
1c65AGLU 11;ASP 20
mutant C54T, C97A, L121A
1c66AGLU 11;ASP 20
mutant C54T, C97A, L121A, L133A
1c67AGLU 11;ASP 20
mutant C54T, C97A, L121A, L133A
1c68AGLU 11;ASP 20
mutant C54T, C97A, L121A, L133A
1c69AGLU 11;ASP 20
mutant C54T, C97A, L133A
1c6aAGLU 11;ASP 20
mutant C54T, C97A, L133A
1c6bAGLU 11;ASP 20
mutant C54T, C97A, L133A
1c6cAGLU 11;ASP 20
mutant C54T, C97A, L99A
1c6dAGLU 11;ASP 20
mutant C54T, C97A, L99A
1c6eAGLU 11;ASP 20
mutant C54T, C97A, L99A
1c6fAGLU 11;ASP 20
mutant C54T, C97A, L99A
1c6gAGLU 11;ASP 20
mutant C54T, C97A, L99A
1c6hAGLU 11;ASP 20
mutant C54T, C97A, L99A
1c6iAGLU 11;ASP 20
mutant C54T, C97A, L99A
1c6jAGLU 11;ASP 20
mutant C54T, C97A, L99A
1c6kAGLU 11;ASP 20
mutant C54T, C97A, L99A
1c6lAGLU 11;ASP 20
mutant C54T, C97A, L99A, F153A
1c6mAGLU 11;ASP 20
mutant C54T, C97A, L99A, F153A
1c6nAGLU 11;ASP 20
mutant C54T, C97A, L99A, F153A
1c6pAGLU 11;ASP 20
mutant C54T, C97A
1c6qAGLU 11;ASP 20
mutant C54T, C97A
1c6tAGLU 11;ASP 20
mutant C54T, C97A
1ctwAGLU 11;ASP 20
mutant I78A
1cu0AGLU 11;ASP 20
mutant I78M
1cu2AGLU 11;ASP 20
mutant I84M
1cu3AGLU 11;ASP 20
mutant V87M
1cu5AGLU 11;ASP 20
mutant L91M
1cu6AGLU 11;ASP 20
mutant L91A
1cupAGLU 11;ASP 20

1cuqAGLU 11;ASP 20
mutant V103M
1cv0AGLU 11;ASP 20
mutant F104M
1cv1AGLU 11;ASP 20
mutant V111M
1cv3AGLU 11;ASP 20
mutant L121M
1cv4AGLU 11;ASP 20
mutant L118M
1cv5AGLU 11;ASP 20
mutant L133M
1cv6AGLU 11;ASP 20
mutant V149M
1cvkAGLU 11;ASP 20
mutant L118A
1cx6AGLU 11;ASP 20

1cx7AGLU 11;ASP 20

1d2wAGLU 11;ASP 20

1d2yAGLU 11;ASP 20

1d3fAGLU 11;ASP 20

1d3jAGLU 11;ASP 20

1d3mAGLU 11;ASP 20

1d3nAGLU 11;ASP 20

1d9wAGLU 11;ASP 20

1dyaAGLU 11;ASP 20
mutant V131D
1dybAGLU 11;ASP 20
mutant V131G
1dycAGLU 11;ASP 20
mutant V131I
1dydAGLU 11;ASP 20
mutant V131L
1dyeAGLU 11;ASP 20
mutant V131S
1dyfAGLU 11;ASP 20
mutant V131M
1dygAGLU 11;ASP 20
mutant V131E
1epyAGLU 11;ASP 20
mutant T21H, C54T, C97A, Q141H, T142H
1l00AGLU 11;ASP 20
mutant Q105A
1l01AGLU 11;ASP 20
mutant T155A, T157I
1l02AGLU 11;ASP 20
mutant T157A
1l03AGLU 11;ASP 20
mutant T157C
1l04AGLU 11;ASP 20
mutant T157D
1l05AGLU 11;ASP 20
mutant T157D
1l06AGLU 11;ASP 20
mutant T157E
1l07AGLU 11;ASP 20
mutant T157F
1l08AGLU 11;ASP 20
mutant T157G
1l09AGLU 11;ASP 20
mutant T157H
1l10AGLU 11;ASP 20
mutant T157I
1l11AGLU 11;ASP 20
mutant T157I
1l12AGLU 11;ASP 20
mutant T157N
1l13AGLU 11;ASP 20
mutant T157R
1l14AGLU 11;ASP 20
mutant T157S
1l15AGLU 11;ASP 20
mutant T157V
1l16AGLU 11;ASP 20
mutant G156D
1l17AGLU 11;ASP 20
mutant I3V
1l18AGLU 11;ASP 20
mutant I3Y
1l19AGLU 11;ASP 20
mutant S38D
1l20AGLU 11;ASP 20
mutant N144D
1l21AGLU 11;ASP 20
mutant N55G
1l22AGLU 11;ASP 20
mutant K124G
1l23AGLU 11;ASP 20
mutant G77A
1l24AGLU 11;ASP 20
mutant A82P
1l25AGLU 11;ASP 20
mutant P86A
1l26AGLU 11;ASP 20
mutant P86C
1l27AGLU 11;ASP 20
mutant P86D
1l28AGLU 11;ASP 20
mutant P86G
1l29AGLU 11;ASP 20
mutant P86H
1l30AGLU 11;ASP 20
mutant P86L
1l31AGLU 11;ASP 20
mutant P86R
1l32AGLU 11;ASP 20
mutant P86S
1l33AGLU 11;ASP 20
mutant V131A
1l34AGLU 11;ASP 20
mutant R96H
1l35AGLU 11;ASP 20
mutant I3Y, I9C, C54T, C97A, L164C
1l36AGLU 11;ASP 20
mutant E128A, V131A, N132A
1l37AGLU 11;ASP 20
mutant T115E
1l38AGLU 11;ASP 20
mutant Q123E
1l39AGLU 11;ASP 20
mutant C54T, C97A, N144E
1l40AGLU 11;ASP 20
mutant C54T, C97A, N144E
1l41AGLU 11;ASP 20
mutant C54T, K83H, C97A, A112D
1l42AGLU 11;ASP 20
mutant K16E
1l43AGLU 11;ASP 20
mutant K16E
1l44AGLU 11;ASP 20
mutant R119E
1l45AGLU 11;ASP 20
mutant K135E
1l46AGLU 11;ASP 20
mutant K147E
1l47AGLU 11;ASP 20
mutant R154E
1l48AGLU 11;ASP 20
mutant A98V
1l49AGLU 11;ASP 20
mutant A98V, T152S
1l50AGLU 11;ASP 20
mutant A98V, V149C, T152S
1l51AGLU 11;ASP 20
mutant A98V, V149I, T152S
1l52AGLU 11;ASP 20
mutant T152S
1l53AGLU 11;ASP 20
mutant V149C
1l54AGLU 11;ASP 20
mutant C54T, C97A, M102K
1l55AGLU 11;ASP 20
mutant C54T, D92N, C97A
1l56AGLU 11;ASP 20
mutant K60P
1l57AGLU 11;ASP 20
mutant N116D
1l58AGLU 11;ASP 20
mutant P143A
1l59AGLU 11;ASP 20
mutant C54T, C97A, T109N
1l60AGLU 11;ASP 20
mutant G113A
1l61AGLU 11;ASP 20
mutant S38N, C54T, C97A
1l62AGLU 11;ASP 20
mutant C54T, C97A, T109D
1l63AGLU 11;ASP 20
mutant C54T, C97A
1l64AGLU 11;ASP 20
mutant N40A, K43A, S44A, E45A, L46A, D47A, K48A, C54T, C97A
1l65AGLU 11;ASP 20
mutant D47A, C54T, C97A
1l66AGLU 11;ASP 20
mutant K43A, C54T, C97A
1l67AGLU 11;ASP 20
mutant L46A, C54T, C97A
1l68AGLU 11;ASP 20
mutant S44A, C54T, C97A
1l69AGLU 11;ASP 20
mutant L133A
1l70AGLU 11;ASP 20
mutant V131A, N132A
1l71AGLU 11;ASP 20
mutant E128A, V131A
1l72AGLU 11;ASP 20
mutant D127A, E128A
1l73AGLU 11;ASP 20
mutant D127A, E128A, V131A, N132A
1l74AGLU 11;ASP 20
mutant E128A, V131A, N132A, L133A
1l75AGLU 11;ASP 20
mutant D127A, E128A, V131A, N132A, L133A
1l76AGLU 11;ASP 20
mutant C54T, D72P, C97A
1l77AGLU 11;ASP 20
mutant C54T, C97A, M102L
1l79AGLU 11;ASP 20
mutant C54T, C97A, L99F, V111I
1l80AGLU 11;ASP 20
mutant C54T, C97A, L99F, M102L, V111I
1l81AGLU 11;ASP 20
mutant C54T, C97A, L99F, M102L, F153L
1l82AGLU 11;ASP 20
mutant C54T, C97A, L99F, M102L, V111I, F153L
1l83AGLU 11;ASP 20
mutant C54T, C97A, L99A
1l84AGLU 11;ASP 20
mutant C54T, C97A, L99A, F153A
1l85AGLU 11;ASP 20
mutant C54T, C97A, F153A
1l86AGLU 11;ASP 20
mutant C54T, C97A, F153I
1l87AGLU 11;ASP 20
mutant C54T, C97A, F153L
1l88AGLU 11;ASP 20
mutant C54T, C97A, F153M
1l89AGLU 11;ASP 20
mutant C54T, C97A, L99A, F153A
1l90AGLU 11;ASP 20
mutant C54T, C97A, L99A
1l91AGLU 11;ASP 20
mutant C54T, C97A, L99F
1l92AGLU 11;ASP 20
mutant C54T, C97A, L99I
1l93AGLU 11;ASP 20
mutant C54T, C97A, L99M
1l94AGLU 11;ASP 20
mutant C54T, C97A, L99V
1l95AGLU 11;ASP 20
mutant C54T, C97A, F153V
1l96AGLU 11;ASP 20
mutant I3P
1l97AGLU 11;ASP 20
mutant I3P
1l97BGLU 11;ASP 20
mutant I3P
1l98AGLU 11;ASP 20
mutant Q105E
1l99AGLU 11;ASP 20
mutant Q105G
1lydAGLU 11;ASP 20
mutant
1lyeAGLU 11;ASP 20
mutant C54T, T59V, C97A
1lyfAGLU 11;ASP 20
mutant C54T, T59S, C97A
1lygAGLU 11;ASP 20
mutant C54T, T59N, C97A
1lyhAGLU 11;ASP 20
mutant C54T, T59G, C97A
1lyiAGLU 11;ASP 20
mutant C54T, T59D, C97A
1lyjAGLU 11;ASP 20
mutant C54T, T59A, C97A
1nhbAGLU 11;ASP 20
mutant C54T, C97A, L99A
1qs5AGLU 11;ASP 20

1qs9AGLU 11;ASP 20

1qsbAGLU 11;ASP 20

1qsqAGLU 11;ASP 20

1qt3AGLU 11;ASP 20
mutant T26D, C54T, C97A
1qt4AGLU 11;ASP 20
mutant T26Q, C54T, C97A
1qt5AGLU 11;      
mutant D20E, C54T, C97A
1qt6A      ;ASP 20
mutant E11H, C54T, C97A
1qt7A      ;ASP 20
mutant E11N, C54T, C97A
1qt8AGLU 11;ASP 20
mutant T26H, C54T, C97A
1qtbAGLU 11;ASP 20

1qtcAGLU 11;ASP 20

1qtdAGLU 11;ASP 20

1qthAGLU 11;ASP 20

1qthBGLU 11;ASP 20

1qtvAGLU 11;ASP 20
mutant T26E, C54T, C97A
1qtzAGLU 11;      
mutant D20C, C54T, C97A
1qudAGLU 11;ASP 20
mutant L99G
1qugAGLU 11;ASP 20
mutant E108V
1quhAGLU 11;ASP 20
mutant L99G, E108V
1quoAGLU 11;ASP 20
mutant L99A, E108V
1tlaAGLU 11;ASP 20
mutant C54T, C97A, S117F
200lAGLU 11;ASP 20
mutant C54T, C97A, L121A
201lAGLU 11;ASP 20
mutant C54T, C97A, insertion K48-HP
201lBGLU 11;ASP 20
mutant C54T, C97A, insertion K48-HP
205lAGLU 11;ASP 20
mutant C54T, C97A, insertion S44-AAA
206lAGLU 11;ASP 20
mutant A42S, C54T, C97A
209lAGLU 11;ASP 20
mutant C54T, C97A, insertion A73-AAA
210lAGLU 11;ASP 20
mutant C54T, C97A, deletion A73
211lAGLU 11;ASP 20
mutant C54T, C97A, insertion E108-A
212lAGLU 11;ASP 20
mutant C54T, C97A, insertion L164-AAAA
213lAGLU 11;ASP 20
mutant C54T, C97A, insertion N140-A
214lAGLU 11;ASP 20
mutant C54T, C97A, insertion R119-A
215lAGLU 11;ASP 20
mutant C54T, C97A, insertion T115-A
216lAGLU 11;ASP 20
mutant S44W, C54T, C97A
216lBGLU 11;ASP 20
mutant S44W, C54T, C97A
217lAGLU 11;ASP 20
mutant S44E, C54T, C97A
218lAGLU 11;ASP 20
mutant C54T, C97A, insertion V131-A
219lAGLU 11;ASP 20
mutant C54T, C97A, insertion L164-AAAA
220lAGLU 11;ASP 20
mutant C54T, C97A, M102A
221lAGLU 11;ASP 20
mutant A49S, C54T, C97A
222lAGLU 11;ASP 20
mutant C54T, C97A, M102A
223lAGLU 11;ASP 20
mutant L133G
224lAGLU 11;ASP 20
mutant C54T, A93S, C97A
225lAGLU 11;ASP 20
mutant L133G
226lAGLU 11;ASP 20
mutant L133G
227lAGLU 11;ASP 20
mutant C54T, C97A, F104A
228lAGLU 11;ASP 20
mutant C54T, C97A, F104A
229lAGLU 11;ASP 20
mutant C54T, R95A, C97A
230lAGLU 11;ASP 20
mutant M6L, C54T, C97A
231lAGLU 11;ASP 20
mutant C54T, C97A, M106K
232lAGLU 11;ASP 20
mutant C54T, C97A, M120K
233lAGLU 11;ASP 20
mutant C54T, C97A, M120L
234lAGLU 11;ASP 20
mutant C54T, C97A, M106L
235lAGLU 11;ASP 20
mutant C54T, C97A, V111A
236lAGLU 11;ASP 20
mutant C54T, V87A, C97A
237lAGLU 11;ASP 20
mutant C54T, C97A, V149A
238lAGLU 11;ASP 20
mutant C54T, C97A, V103A
239lAGLU 11;ASP 20
mutant I17A, C54T, C97A
240lAGLU 11;ASP 20
mutant I27A, C54T, C97A
241lAGLU 11;ASP 20
mutant I29A, C54T, C97A
242lAGLU 11;ASP 20
mutant I50A, C54T, C97A
243lAGLU 11;ASP 20
mutant C54T, I58A, C97A
244lAGLU 11;ASP 20
mutant C54T, C97A, I100A
245lAGLU 11;ASP 20
mutant M6A, C54T, C97A
246lAGLU 11;ASP 20
mutant C54T, F67A, C97A
247lAGLU 11;ASP 20
mutant C54T, L84A, C97A
248lAGLU 11;ASP 20
mutant I27A, I29A, C54T, C97A
249lAGLU 11;ASP 20
mutant I27A, C54T, I58A, C97A
250lAGLU 11;ASP 20
mutant I29A, C54T, I58A, C97A
251lAGLU 11;ASP 20
mutant C54T, C97A, L121A, L133A
252lAGLU 11;ASP 20
mutant C54T, C97A, M102A, M106A
253lAGLU 11;      
mutant D20A, C54T, C97A
254lAGLU 11;      
mutant D20S, C54T, C97A
255lAGLU 11;      
mutant D20N, C54T, C97A
256lAGLU 11;ASP 20
mutant M6I
257lAGLU 11;ASP 20
mutant C54T, C97A
258lAGLU 11;ASP 20
mutant
259lAGLU 11;ASP 20
mutant T21H, C54T, C97A, T142H
260lAGLU 11;ASP 20
mutant T21H, C54T, C97A, T142H
262lAGLU 11;ASP 20
mutant L39I, insertion I50-NAAKSELDKAI
262lBGLU 11;ASP 20
mutant L39I, insertion I50-NAAKSELDKAI
2l78AGLU 11;ASP 20
mutant C54T, C97A, V111I
2lzmAGLU 11;ASP 20
mutant
3lzmAGLU 11;ASP 20
mutant
4lzmAGLU 11;ASP 20
mutant
5lzmAGLU 11;ASP 20
mutant
6lzmAGLU 11;ASP 20
mutant
7lzmAGLU 11;ASP 20
mutant

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]

[4]

[24]Fig.1, p.9461-94632
[50]Fig.3
[52]p.6787
[59]

[61]Fig.3, p.1007
[64]Fig.2, p.58
[77]Fig.4, p.8951-8953

references
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CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID77157239
PubMed ID322662
JournalBiochem Biophys Res Commun
Year1977
Volume75
Pages265-70
AuthorsRemington SJ, Eyck LF, Matthews BW
TitleAtomic coordinates for T4 phage lysozyme.
Related Swiss-protP00720
[2]
PubMed ID7308203
JournalEur J Biochem
Year1981
Volume119
Pages589-93
AuthorsKleppe G, Vasstrand E, Jensen HB
TitleThe specificity requirements of bacteriophage T4 lysozyme. Involvement of N-acetamido groups.
[3]
PubMed ID7277499
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Year1981
Volume147
Pages523-43
AuthorsAnderson WF, Grutter MG, Remington SJ, Weaver LH, Matthews BW
TitleCrystallographic determination of the mode of binding of oligosaccharides to T4 bacteriophage lysozyme: implications for the mechanism of catalysis.
[4]
PubMed ID7207627
JournalNature
Year1981
Volume290
Pages334-5
AuthorsMatthews BW, Grutter MG, Anderson WF, Remington SJ
TitleCommon precursor of lysozymes of hen egg-white and bacteriophage T4.
[5]
PubMed ID7077670
JournalJ Mol Biol
Year1982
Volume154
Pages525-35
AuthorsGrutter MG, Matthews BW
TitleAmino acid substitutions far from the active site of bacteriophage T4 lysozyme reduce catalytic activity and suggest that the C-terminal lobe of the enzyme participates in substrate binding.
[6]
CommentsX-ray crystallography
PubMed ID3680274
JournalJ Biol Chem
Year1987
Volume262
Pages16858-64
AuthorsGray TM, Matthews BW
TitleStructural analysis of the temperature-sensitive mutant of bacteriophage T4 lysozyme, glycine 156----aspartic acid.
Related PDB1l16
[7]
CommentsX-ray crystallography
PubMed ID3681997
JournalJ Mol Biol
Year1987
Volume197
Pages315-29
AuthorsGrutter MG, Gray TM, Weaver LH, Wilson TA, Matthews BW
TitleStructural studies of mutants of the lysozyme of bacteriophage T4. The temperature-sensitive mutant protein Thr157----Ile.
Related PDB1l01,1l10
[8]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
Medline ID87226186
PubMed ID3586019
JournalJ Mol Biol
Year1987
Volume193
Pages189-99
AuthorsWeaver LH, Matthews BW
TitleStructure of bacteriophage T4 lysozyme refined at 1.7 A resolution.
Related PDB2lzm
Related Swiss-protP00720
[9]
CommentsX-ray crystallography
PubMed ID3118211
JournalNature
Year1987
Volume330
Pages41-6
AuthorsAlber T, Sun DP, Wilson K, Wozniak JA, Cook SP, Matthews BW
TitleContributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.
Related PDB1l02,1l03,1l04,1l05,1l06,1l07,1l08,1l09,1l11,1l12,1l13,1l14,1l15,1l14
[10]
CommentsX-ray crystallography
PubMed ID3477797
JournalProc Natl Acad Sci U S A
Year1987
Volume84
Pages6663-7
AuthorsMatthews BW, Nicholson H, Becktel WJ
TitleEnhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
Related PDB1l23,1l24
[11]
PubMed ID3029773
JournalProc Natl Acad Sci U S A
Year1987
Volume84
Pages1244-8
AuthorsMcIntosh LP, Griffey RH, Muchmore DC, Nielson CP, Redfield AG, Dahlquist FW
TitleProton NMR measurements of bacteriophage T4 lysozyme aided by 15N isotopic labeling: structural and dynamic studies of larger proteins.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT ILE-3.
Medline ID88302415
PubMed ID3405287
JournalNature
Year1988
Volume334
Pages406-10
AuthorsMatsumura M, Becktel WJ, Matthews BW
TitleHydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3.
Related PDB1l17,1l18
Related Swiss-protP00720
[13]
CommentsX-ray crystallography
PubMed ID3200317
JournalNature
Year1988
Volume336
Pages651-6
AuthorsNicholson H, Becktel WJ, Matthews BW
TitleEnhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
Related PDB1l19,1l20
[14]
CommentsX-ray crystallography
PubMed ID3074306
JournalProtein Eng
Year1988
Volume2
Pages277-82
AuthorsRose DR, Phipps J, Michniewicz J, Birnbaum GI, Ahmed FR, Muir A, Anderson WF, Narang S
TitleCrystal structure of T4-lysozyme generated from synthetic coding DNA expressed in Escherichia coli.
Related PDB1lyd
[15]
CommentsX-ray crystallography
PubMed ID3277275
JournalScience
Year1988
Volume239
Pages631-5
AuthorsAlber T, Bell JA, Sun DP, Nicholson H, Wozniak JA, Cook S, Matthews BW
TitleReplacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability.
Related PDB1l25,1l26,1l27,1l28,1l29,1l30,1l31,1l32
[16]
CommentsX-ray crystallography
PubMed ID2665808
JournalBiochemistry
Year1989
Volume28
Pages3793-7
AuthorsWeaver LH, Gray TM, Grutter MG, Anderson DE, Wozniak JA, Dahlquist FW, Matthews BW
TitleHigh-resolution structure of the temperature-sensitive mutant of phage lysozyme, Arg 96----His.
Related PDB1l34
[17]
CommentsX-ray crystallography
PubMed ID2674124
JournalJ Biol Chem
Year1989
Volume264
Pages16059-66
AuthorsMatsumura M, Wozniak JA, Sun DP, Matthews BW
TitleStructural studies of mutants of T4 lysozyme that alter hydrophobic stabilization.
Related PDB3lzm
[18]
CommentsX-ray crystallography
PubMed ID2511328
JournalJ Mol Biol
Year1989
Volume210
Pages181-93
AuthorsNicholson H, Soderlind E, Tronrud DE, Matthews BW
TitleContributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozyme.
Related PDB1l21,1l22,1l33
[19]
CommentsX-ray crystallography
PubMed ID2916125
JournalScience
Year1989
Volume243
Pages792-4
AuthorsMatsumura M, Matthews BW
TitleControl of enzyme activity by an engineered disulfide bond.
Related PDB155l,156l,157l,158l,159l,160l,161l,162l,163l,164l,165l,166l
[20]
CommentsSTRUCTURE BY NMR.
Medline ID91002526
PubMed ID2207079
JournalBiochemistry
Year1990
Volume29
Pages6341-62
AuthorsMcIntosh LP, Wand AJ, Lowry DF, Redfield AG, Dahlquist FW
TitleAssignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme.
Related Swiss-protP00720
[21]
CommentsX-ray crystallography
PubMed ID2334683
JournalBiochemistry
Year1990
Volume29
Pages2592-8
AuthorsPjura PE, Matsumura M, Wozniak JA, Matthews BW
TitleStructure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein.
Related PDB1l35
[22]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT.
Medline ID91043097
PubMed ID2234094
JournalNature
Year1990
Volume348
Pages263-6
AuthorsFaber HR, Matthews BW
TitleA mutant T4 lysozyme displays five different crystal conformations.
Related PDB256l
Related Swiss-protP00720
[23]
CommentsX-ray crystallography
PubMed ID1747370
JournalBiochemistry
Year1991
Volume30
Pages11521-9
AuthorsDao-pin S, Anderson DE, Baase WA, Dahlquist FW, Matthews BW
TitleStructural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme.
Related PDB1l54
[24]
PubMed ID1892846
JournalBiochemistry
Year1991
Volume30
Pages9457-63
AuthorsHardy LW, Poteete AR
TitleReexamination of the role of Asp20 in catalysis by bacteriophage T4 lysozyme.
[25]
CommentsX-ray crystallography
PubMed ID1911773
JournalBiochemistry
Year1991
Volume30
Pages9816-28
AuthorsNicholson H, Anderson DE, Dao-pin S, Matthews BW
TitleAnalysis of the interaction between charged side chains and the alpha-helix dipole using designed thermostable mutants of phage T4 lysozyme.
Related PDB1l55,1l57,1l59,1l61,1l62,1l63
[26]
PubMed ID1991123
JournalBiochemistry
Year1991
Volume30
Pages1425-32
AuthorsPoteete AR, Sun DP, Nicholson H, Matthews BW
TitleSecond-site revertants of an inactive T4 lysozyme mutant restore activity by restructuring the active site cleft.
[27]
CommentsX-ray crystallography
PubMed ID1854726
JournalBiochemistry
Year1991
Volume30
Pages7142-53
AuthorsSun DP, Sauer U, Nicholson H, Matthews BW
TitleContributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis.
Related PDB1l37,1l38,1l39,1l40,1l41
[28]
CommentsX-ray crystallography
PubMed ID1998663
JournalBiochemistry
Year1991
Volume30
Pages2012-7
AuthorsZhang XJ, Baase WA, Matthews BW
TitleToward a simplification of the protein folding problem: a stabilizing polyalanine alpha-helix engineered in T4 lysozyme.
Related PDB1l36
[29]
PubMed ID1814699
JournalCiba Found Symp
Year1991
Volume161
Pages91-103; discussion 103-7
AuthorsKollman PA, Daggett V, Dang LX
TitleThe application of computational methods to the study of enzyme catalysis by triose-phosphate isomerase and stabilities of variants of bacteriophage T4 lysozyme.
[30]
CommentsX-ray crystallography
PubMed ID1920439
JournalJ Mol Biol
Year1991
Volume221
Pages647-67
AuthorsDaopin S, Alber T, Baase WA, Wozniak JA, Matthews BW
TitleStructural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme.
Related PDB1l48,1l49,1l50,1l51,1l52,1l53
[31]
CommentsX-ray crystallography
PubMed ID1942034
JournalJ Mol Biol
Year1991
Volume221
Pages873-87
AuthorsSun DP, Soderlind E, Baase WA, Wozniak JA, Sauer U, Matthews BW
TitleCumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
Related PDB1l42,1l43,1l44,1l45,1l46,1l47,1l58
[32]
CommentsX-ray crystallography
PubMed ID2062826
JournalProteins
Year1991
Volume10
Pages10-21
AuthorsBell JA, Wilson KP, Zhang XJ, Faber HR, Nicholson H, Matthews BW
TitleComparison of the crystal structure of bacteriophage T4 lysozyme at low, medium, and high ionic strengths.
Related PDB4lzm,5lzm,6lzm,7lzm
[33]
CommentsX-ray crystallography
PubMed ID1567817
JournalBiochemistry
Year1992
Volume31
Pages3590-6
AuthorsBell JA, Becktel WJ, Sauer U, Baase WA, Matthews BW
TitleDissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at Thr 59.
Related PDB1lye,1lyf,1lyg,1lyh,1lyi,1lyj
[34]
CommentsX-ray crystallography
PubMed ID1457724
JournalBiopolymers
Year1992
Volume32
Pages1431-41
AuthorsNicholson H, Tronrud DE, Becktel WJ, Matthews BW
TitleAnalysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozyme.
Related PDB1l56,1l60
[35]
CommentsX-ray crystallography
PubMed ID1733941
JournalJ Biol Chem
Year1992
Volume267
Pages2393-9
AuthorsSauer UH, San DP, Matthews BW
TitleTolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesions.
Related PDB1l76
[36]
CommentsX-ray crystallography
PubMed ID1404394
JournalJ Mol Biol
Year1992
Volume227
Pages917-33
AuthorsDixon MM, Nicholson H, Shewchuk L, Baase WA, Matthews BW
TitleStructure of a hinge-bending bacteriophage T4 lysozyme mutant, Ile3-->Pro.
Related PDB1l96,1l97
[37]
CommentsX-ray crystallography
PubMed ID1569571
JournalJ Mol Biol
Year1992
Volume224
Pages1143-59
AuthorsHurley JH, Baase WA, Matthews BW
TitleDesign and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme.
Related PDB1l77,1l79,1l80,1l81,1l82,2l78
[38]
CommentsX-RAY CRYSTALLOGRAPHY OF MUTANT.
Medline ID92115004
PubMed ID1731252
JournalNature
Year1992
Volume355
Pages371-3
AuthorsEriksson AE, Baase WA, Wozniak JA, Matthews BW
TitleA cavity-containing mutant of T4 lysozyme is stabilized by buried benzene.
Related PDB1l83,1l84
Related Swiss-protP00720
[39]
CommentsX-ray crystallography
PubMed ID1570293
JournalProc Natl Acad Sci U S A
Year1992
Volume89
Pages3751-5
AuthorsHeinz DW, Baase WA, Matthews BW
TitleFolding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence.
Related PDB1l64,1l65,1l66,1l67,1l68
[40]
CommentsX-ray crystallography
PubMed ID1304882
JournalProtein Sci
Year1992
Volume1
Pages46-57
AuthorsJacobson RH, Matsumura M, Faber HR, Matthews BW
TitleStructure of a stabilizing disulfide bridge mutant that closes the active-site cleft of T4 lysozyme.
Related PDB259l,1kni
[41]
CommentsX-ray crystallography
PubMed ID1304917
JournalProtein Sci
Year1992
Volume1
Pages761-76
AuthorsZhang XJ, Baase WA, Matthews BW
TitleMultiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability.
Related PDB1l69,1l70,1l71,1l72,1l73,1l74,1l75
[42]
CommentsX-ray crystallography
PubMed ID8218201
JournalBiochemistry
Year1993
Volume32
Pages11363-73
AuthorsBlaber M, Lindstrom JD, Gassner N, Xu J, Heinz DW, Matthews BW
TitleEnergetic cost and structural consequences of burying a hydroxyl group within the core of a protein determined from Ala-->Ser and Val-->Thr substitutions in T4 lysozyme.
Related PDB118l,119l,120l,122l,123l,125l,126l,127l,128l,206l,221l,224l
[43]
CommentsX-ray crystallography
PubMed ID8433369
JournalJ Mol Biol
Year1993
Volume229
Pages747-69
AuthorsEriksson AE, Baase WA, Matthews BW
TitleSimilar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences.
Related PDB1l85,1l86,1l87,1l88,1l89,1l90,1l91,1l92,1l93,1l94,1l95
[44]
CommentsX-ray crystallography
PubMed ID8429913
JournalNature
Year1993
Volume361
Pages561-4
AuthorsHeinz DW, Baase WA, Dahlquist FW, Matthews BW
TitleHow amino-acid insertions are allowed in an alpha-helix of T4 lysozyme.
Related PDB102l,103l,104l,201l,205l
[45]
CommentsX-ray crystallography
PubMed ID8401213
JournalProtein Sci
Year1993
Volume2
Pages1285-90
AuthorsAnderson DE, Hurley JH, Nicholson H, Baase WA, Matthews BW
TitleHydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-->Phe.
Related PDB1tla
[46]
CommentsX-ray crystallography
PubMed ID8298466
JournalProtein Sci
Year1993
Volume2
Pages2226-32
AuthorsPjura P, Matthews BW
TitleStructures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent.
Related PDB129l,130l,131l
[47]
CommentsX-ray crystallography
PubMed ID8460110
JournalProteins
Year1993
Volume15
Pages401-12
AuthorsPjura P, McIntosh LP, Wozniak JA, Matthews BW
TitlePerturbation of Trp 138 in T4 lysozyme by mutations at Gln 105 used to correlate changes in structure, stability, solvation, and spectroscopic properties.
Related PDB1l00,1l98,1l99
[48]
CommentsX-ray crystallography
PubMed ID8259514
JournalScience
Year1993
Volume262
Pages1715-8
AuthorsBaldwin EP, Hajiseyedjavadi O, Baase WA, Matthews BW
TitleThe role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme.
Related PDB140l,141l,142l,143l,144l,145l,146l,147l
[49]
CommentsX-ray crystallography
PubMed ID8503008
JournalScience
Year1993
Volume260
Pages1637-40
AuthorsBlaber M, Zhang XJ, Matthews BW
TitleStructural basis of amino acid alpha helix propensity.
Related PDB107l,108l,109l,110l,111l,112l,113l,114l,115l,116l,137l,216l,217l
[50]
CommentsX-ray crystallography
PubMed ID8266098
JournalScience
Year1993
Volume262
Pages2030-3
AuthorsKuroki R, Weaver LH, Matthews BW
TitleA covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme.
Related PDB148l
[51]
PubMed ID7727368
JournalBiochemistry
Year1994
Volume33
Pages11174-83
AuthorsMcLeish MJ, Nielsen KJ, Najbar LV, Wade JD, Lin F, Doughty MB, Craik DJ
TitleConformation of a peptide corresponding to T4 lysozyme residues 59-81 by NMR and CD spectroscopy.
[52]
PubMed ID7961435
JournalJ Bacteriol
Year1994
Volume176
Pages6783-8
AuthorsPoteete AR, Hardy LW
TitleGenetic analysis of bacteriophage T4 lysozyme structure and function.
[53]
CommentsX-ray crystallography
PubMed ID8289284
JournalJ Mol Biol
Year1994
Volume235
Pages600-24
AuthorsBlaber M, Zhang XJ, Lindstrom JD, Pepiot SD, Baase WA, Matthews BW
TitleDetermination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme.
Related PDB1dya,1dyb,1dyc,1dyd,1dye,1dyf,1dyg
[54]
PubMed ID8114100
JournalJ Mol Biol
Year1994
Volume236
Pages869-86
AuthorsHeinz DW, Baase WA, Zhang XJ, Blaber M, Dahlquist FW, Matthews BW
TitleAccommodation of amino acid insertions in an alpha-helix of T4 lysozyme. Structural and thermodynamic analysis.
[55]
CommentsX-ray crystallography
PubMed ID8177878
JournalProtein Eng
Year1994
Volume7
Pages301-7
AuthorsHeinz DW, Matthews BW
TitleRapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking.
Related PDB138l,139l
[56]
CommentsX-ray crystallography
PubMed ID7920248
JournalProtein Sci
Year1994
Volume3
Pages1031-9
AuthorsZhang XJ, Matthews BW
TitleConservation of solvent-binding sites in 10 crystal forms of T4 lysozyme.
Related PDB149l,150l,151l,152l
[57]
CommentsX-ray crystallography
PubMed ID7612599
JournalBiochemistry
Year1995
Volume34
Pages8576-88
AuthorsMorton A, Matthews BW
TitleSpecificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity.
Related PDB181l,182l,183l,184l,185l,186l,187l,188l,1nhb
[58]
PubMed ID7632721
JournalBiochim Biophys Acta
Year1995
Volume1250
Pages163-70
AuthorsNajbar LV, Craik DJ, Wade JD, Lin F, McLeish MJ
TitleCD and NMR determination of the solution structure of a peptide corresponding to T4 lysozyme residues 38-51.
[59]
PubMed ID7823320
JournalJ Mol Biol
Year1995
Volume245
Pages54-68
AuthorsWeaver LH, Grutter MG, Matthews BW
TitleThe refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue.
[60]
CommentsX-ray crystallography
PubMed ID7616572
JournalJ Mol Biol
Year1995
Volume250
Pages527-52
AuthorsZhang XJ, Wozniak JA, Matthews BW
TitleProtein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme.
Related PDB167l,168l,169l,170l,171l,172l,173l,174l,175l,176l,177l,178l,179l,180l
[61]
PubMed ID7583653
JournalNat Struct Biol
Year1995
Volume2
Pages1007-11
AuthorsKuroki R, Weaver LH, Matthews BW
TitleStructure-based design of a lysozyme with altered catalytic activity.
[62]
CommentsX-ray crystallography
PubMed ID7831309
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages452-6
AuthorsShoichet BK, Baase WA, Kuroki R, Matthews BW
TitleA relationship between protein stability and protein function.
Related PDB253l,254l,255l
[63]
CommentsX-ray crystallography
PubMed ID8771182
JournalProtein Eng
Year1995
Volume8
Pages1017-22
AuthorsZhang XJ, Baase WA, Shoichet BK, Wilson KP, Matthews BW
TitleEnhancement of protein stability by the combination of point mutations in T4 lysozyme is additive.
Related PDB189l
[64]
PubMed ID8958073
JournalAnn N Y Acad Sci
Year1996
Volume799
Pages56-60
AuthorsMorimoto K, Kuroki R, Matthews BW
TitleControl of the catalytic mechanism of an enzyme by amino acid substitution.
[65]
CommentsX-ray crystallography
PubMed ID8676387
JournalJ Mol Biol
Year1996
Volume259
Pages542-59
AuthorsBaldwin E, Xu J, Hajiseyedjavadi O, Baase WA, Matthews BW
TitleThermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme.
Related PDB195l,196l,197l,198l,199l,200l
[66]
CommentsX-ray crystallography
PubMed ID8976549
JournalProtein Sci
Year1996
Volume5
Pages2399-415
AuthorsVetter IR, Baase WA, Heinz DW, Xiong JP, Snow S, Matthews BW
TitleProtein structural plasticity exemplified by insertion and deletion mutants in T4 lysozyme.
Related PDB209l,210l,211l,212l,213l,214l,215l,218l,219l
[67]
PubMed ID9003182
JournalBiochemistry
Year1997
Volume36
Pages307-16
AuthorsMchaourab HS, Oh KJ, Fang CJ, Hubbell WL
TitleConformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling.
[68]
PubMed ID10099305
JournalBiotechnol Bioeng
Year1998
Volume58
Pages658-62
AuthorsBower CK, Xu Q, McGuire J
TitleActivity losses among T4 lysozyme variants after adsorption to colloidal silica.
[69]
CommentsX-ray crystallography
PubMed ID9514755
JournalJ Mol Biol
Year1998
Volume277
Pages467-85
AuthorsBaldwin E, Baase WA, Zhang X, Feher V, Matthews BW
TitleGeneration of ligand binding sites in T4 lysozyme by deficiency-creating substitutions.
Related PDB220l,222l,223l,225l,226l,227l,228l,229l,252l
[70]
PubMed ID9514719
JournalJ Mol Biol
Year1998
Volume276
Pages151-64
AuthorsEvrard C, Fastrez J, Declercq JP
TitleCrystal structure of the lysozyme from bacteriophage lambda and its relationship with V and C-type lysozymes.
[71]
CommentsX-ray crystallography
PubMed ID9541409
JournalProtein Sci
Year1998
Volume7
Pages765-73
AuthorsLipscomb LA, Gassner NC, Snow SD, Eldridge AM, Baase WA, Drew DL, Matthews BW
TitleContext-dependent protein stabilization by methionine-to-leucine substitution shown in T4 lysozyme.
Related PDB230l,231l,232l,233l,234l
[72]
CommentsX-ray crystallography
PubMed ID9514271
JournalProtein Sci
Year1998
Volume7
Pages158-77
AuthorsXu J, Baase WA, Baldwin E, Matthews BW
TitleThe response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect.
Related PDB235l,236l,237l,238l,239l,240l,241l,242l,243l,244l,245l,246l,247l,248l,249l,250l,251l
[73]
CommentsX-ray crystallography
PubMed ID10545167
JournalBiochemistry
Year1999
Volume38
Pages14451-60
AuthorsGassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW
TitleMethionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.
Related PDB1ctw,1cu0,1cu2,1cu3,1cu5,1cu6,1cup,1cuq,1cv0,1cv1,1cv3,1cv4,1cv5,1cv6,1cvk,1cx7,1qsq
[74]
PubMed ID10074347
JournalBiochemistry
Year1999
Volume38
Pages2947-55
AuthorsMchaourab HS, Kalai T, Hideg K, Hubbell WL
TitleMotion of spin-labeled side chains in T4 lysozyme: effect of side chain structure.
[75]
CommentsX-ray crystallography
PubMed ID10556025
JournalJ Mol Biol
Year1999
Volume294
Pages17-20
AuthorsGassner NC, Baase WA, Hausrath AC, Matthews BW
TitleSubstitution with selenomethionine can enhance the stability of methionine-rich proteins.
Related PDB1cx6,1d2w,1d2y,1d3f,1d3j,1d3m,1d3n
[76]
CommentsX-ray crystallography
PubMed ID10512706
JournalJ Mol Biol
Year1999
Volume292
Pages1111-20
AuthorsWray JW, Baase WA, Lindstrom JD, Weaver LH, Poteete AR, Matthews BW
TitleStructural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability.
Related PDB1qud,1qug,1quh,1quo
[77]
CommentsX-ray crystallography
PubMed ID10430876
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages8949-54
AuthorsKuroki R, Weaver LH, Matthews BW
TitleStructural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site.
Related PDB1qt3,1qt4,1qt5,1qt6,1qt7,1qt8,1qtv,1qtz
[78]
CommentsX-ray crystallography
PubMed ID10339544
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages6078-83
AuthorsSagermann M, Baase WA, Matthews BW
TitleStructural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein folding.
Related PDB262l,261l
[79]
CommentsX-ray crystallography
PubMed ID10623513
JournalJ Mol Biol
Year2000
Volume295
Pages127-45
AuthorsLiu R, Baase WA, Matthews BW
TitleThe introduction of strain and its effects on the structure and stability of T4 lysozyme.
Related PDB1qs5,1qs9,1qsb,1qtb,1qtc,1qtd,1qth
[80]
CommentsX-ray crystallography
PubMed ID10993735
JournalJ Mol Biol
Year2000
Volume302
Pages955-77
AuthorsQuillin ML, Breyer WA, Griswold IJ, Matthews BW
TitleSize versus polarizability in protein-ligand interactions: binding of noble gases within engineered cavities in phage T4 lysozyme.
Related PDB1c60,1c61,1c62,1c63,1c64,1c65,1c66,1c67,1c68,1c69,1c6a,1c6b,1c6c,1c6d,1c6e,1c6f,1c6g,1c6h,1c6i,1c6j,1c6k,1c6l,1c6m,1c6n,1c6p,1c6q,1c6t
[81]
CommentsX-ray crystallography
PubMed ID10618384
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages139-44
AuthorsYang G, Cecconi C, Baase WA, Vetter IR, Breyer WA, Haack JA, Matthews BW, Dahlquist FW, Bustamante C
TitleSolid-state synthesis and mechanical unfolding of polymers of T4 lysozyme.
Related PDB1b6i
[82]
CommentsX-ray crystallography
PubMed ID10835104
JournalProtein Eng
Year2000
Volume13
Pages313-21
AuthorsWray JW, Baase WA, Ostheimer GJ, Zhang XJ, Matthews BW
TitleUse of a non-rigid region in T4 lysozyme to design an adaptable metal-binding site.
Related PDB1epy,257l,258l,260l
[83]
PubMed ID11300763
JournalBiochemistry
Year2001
Volume40
Pages3828-46
AuthorsColumbus L, Kalai T, Jeko J, Hideg K, Hubbell WL
TitleMolecular motion of spin labeled side chains in alpha-helices: analysis by variation of side chain structure.
[84]
PubMed ID11341831
JournalBiochemistry
Year2001
Volume40
Pages5665-73
AuthorsLeung AK, Duewel HS, Honek JF, Berghuis AM
TitleCrystal structure of the lytic transglycosylase from bacteriophage lambda in complex with hexa-N-acetylchitohexaose.
[85]
PubMed ID11350172
JournalJ Mol Biol
Year2001
Volume308
Pages745-64
AuthorsGoto NK, Skrynnikov NR, Dahlquist FW, Kay LE
TitleWhat is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR.
[86]
CommentsX-ray crystallography
PubMed ID11316887
JournalProtein Sci
Year2001
Volume10
Pages1067-78
AuthorsXu J, Baase WA, Quillin ML, Baldwin EP, Matthews BW
TitleStructural and thermodynamic analysis of the binding of solvent at internal sites in T4 lysozyme.
Related PDB1g06,1g07,1g0g,1g0j,1g0k,1g0l,1g0m,1g0p,1g0q,1g1v,1g1w,1i6s
[87]
CommentsX-ray crystallography
PubMed ID12487988
JournalBiophys Chem
Year2002
Volume101-102
Pages43-56
AuthorsZhang X, Baase WA, Matthews BW
TitleA helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis.
Related PDB190l,191l,192l,1d9w
[88]
PubMed ID11996571
JournalJ Am Chem Soc
Year2002
Volume124
Pages5304-14
AuthorsBorbat PP, McHaourab HS, Freed JH
TitleProtein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme.
[89]
PubMed ID11841314
JournalJ Am Chem Soc
Year2002
Volume124
Pages1443-51
AuthorsMulder FA, Hon B, Mittermaier A, Dahlquist FW, Kay LE
TitleSlow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme.
[90]
CommentsX-ray crystallography
PubMed ID11884133
JournalJ Mol Biol
Year2002
Volume316
Pages931-40
AuthorsSagermann M, Matthews BW
TitleCrystal structures of a T4-lysozyme duplication-extension mutant demonstrate that the highly conserved beta-sheet region has low intrinsic folding propensity.
Related PDB1jtm
[91]
CommentsX-ray crystallography
PubMed ID12217695
JournalJ Mol Biol
Year2002
Volume322
Pages339-55
AuthorsWei BQ, Baase WA, Weaver LH, Matthews BW, Shoichet BK
TitleA model binding site for testing scoring functions in molecular docking.
Related PDB1lgu,1lgw,1lgx,1li2,1li3,1li6
[92]
PubMed ID12364581
JournalProtein Eng
Year2002
Volume15
Pages669-75
AuthorsMachicado C, Bueno M, Sancho J
TitlePredicting the structure of protein cavities created by mutation.
[93]
CommentsX-ray crystallography
PubMed ID11847274
JournalProtein Sci
Year2002
Volume11
Pages516-21
AuthorsSagermann M, Martensson LG, Baase WA, Matthews BW
TitleA test of proposed rules for helix capping: implications for protein design.
Related PDB1jqu,1llh
[94]
CommentsX-ray crystallography
PubMed ID12646375
JournalBiophys Chem
Year2003
Volume100
Pages325-40
AuthorsGassner NC, Baase WA, Mooers BH, Busam RD, Weaver LH, Lindstrom JD, Quillin ML, Matthews BW
TitleMultiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability.
Related PDB1ks3,1kw5,1kw7,1ky0,1ky1,1l0j,1l0k,1lpy,1lw9,1lwg,1lwk
[95]
PubMed ID12770868
JournalBiophys J
Year2003
Volume84
Pages3583-93
AuthorsZhang Z, Shi Y, Liu H
TitleMolecular dynamics simulations of peptides and proteins with amplified collective motions.
[96]
CommentsX-ray crystallography
PubMed ID12963380
JournalJ Mol Biol
Year2003
Volume332
Pages741-56
AuthorsMooers BH, Datta D, Baase WA, Zollars ES, Mayo SL, Matthews BW
TitleRepacking the Core of T4 lysozyme by automated design.
Related PDB1p2l,1p2r,1p36,1p37,1p3n,1p46,1p64,1p6y,1p7s,1pqd,1pqi,1pqj,1pqk,1pqm,1pqo
[97]
CommentsX-ray crystallography
PubMed ID12869697
JournalProc Natl Acad Sci U S A
Year2003
Volume100
Pages9191-5
AuthorsSagermann M, Gay L, Matthews BW
TitleLong-distance conformational changes in a protein engineered by modulated sequence duplication
Related PDB1oyu
[98]
PubMed ID14756565
JournalBiochemistry
Year2004
Volume43
Pages1296-301
AuthorsSagermann M, Baase WA, Mooers BH, Gay L, Matthews BW
TitleRelocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding.

comments
This enzyme belongs to the glycosidase family-24, which seems to have an inverting mechanism. It converts the configuration of substrate saccharide from equatorial one (or beta-anomer) to axial conformation (or alpha-anomer) (see [77]).
According to the literature [61], [64] & [77], the catalytic reaction proceeds in a single displacement mechanism, as follows:
(1) Asp20 acts as a general base to acitivate a nearby water molecule.
(2) The activated water makes a nucleophilic attack on the C1-atom of glycosidic bond, releasing an alpha-anomer, whilst Glu11 acts as a general acid to protonate the oxygen atom of the glycosidic bond, resulting in the formation of alpha-anomer product.
However, the paper [77] suggested that Asp20 is not so essential as Glu11. A counterpart of this residue in Goose lysozyme does not exist (see [59]).
In contrast to the wild-type enzyme, the mutant T26H has got a double displacement mechanism, in which the mutated residue, His26, acts as a nucleophile to form a covalent-bonded intermediate, releasing beta-anomer products (see [61], [64] & [77]).

createdupdated
2004-09-272009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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