EzCatDB: S00509

DB codeS00509
RLCP classification1.30.33100.2
CATH domainDomain 11.10.530.10Catalytic domain
E.C.3.2.1.17
CSA135l

CATH domainRelated DB codes (homologues)
1.10.530.10S00520,D00170

Enzyme Name
Swiss-protKEGG

P00698P00700P00704P00702P00703
Protein nameLysozyme C (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase C) (Allergen Gal d IV)AltName: Allergen=Gal d 4;Lysozyme CLysozyme CLysozyme CLysozyme Clysozyme
muramidase
globulin G
mucopeptide glucohydrolase
globulin G1
N,O-diacetylmuramidase
lysozyme g
L-7001
1,4-N-acetylmuramidase
mucopeptide N-acetylmuramoylhydrolase
PR1-lysozyme
SynonymsNoneEC 3.2.1.17
1,4-beta-N-acetylmuramidase C
EC 3.2.1.17
1,4-beta-N-acetylmuramidase C
EC 3.2.1.17
1,4-beta-N-acetylmuramidase C
EC 3.2.1.17
1,4-beta-N-acetylmuramidase C


Swiss-prot:Accession NumberP00698P00700P00704P00702P00703
Entry nameLYSC_CHICKLYSC_COLVILYSC_NUMMELYSC_PHACOLYSC_MELGA
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.Hydrolysis 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.Hydrolysis 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.Hydrolysis 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.Hydrolysis 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.
SubunitMonomer.Monomer.Monomer.Monomer.Monomer.
Subcellular location




Cofactor






SubstratesProducts
KEGG-idC00889C00851C00001C04394C00851C00140
CompoundPeptidoglycanChitodextrinH2OPeptidoglycan(N-acetyl-D-glucosamine)ChitodextrinN-Acetyl-D-glucosamine
Typeamino acids,amide group,amine group,carbohydrate,peptide/protein,polysaccharideamide group,polysaccharideH2Oamino acids,amide group,amine group,carbohydrate,lipid,peptide/protein,polysaccharideamide group,polysaccharideamide group,carbohydrate
1a2yCUnboundUnbound
UnboundUnboundUnbound
1at5AUnboundUnbound
UnboundBound:NAG-NAG-NAGUnbound
1at6AUnboundUnbound
UnboundBound:NAG-NAG-NAGUnbound
1bvkCUnboundUnbound
UnboundUnboundUnbound
1bvkFUnboundUnbound
UnboundUnboundUnbound
1dqjCUnboundUnbound
UnboundUnboundUnbound
1fdlYUnboundUnbound
UnboundUnboundUnbound
1g7hCUnboundUnbound
UnboundUnboundUnbound
1g7iCUnboundUnbound
UnboundUnboundUnbound
1g7jCUnboundUnbound
UnboundUnboundUnbound
1g7lCUnboundUnbound
UnboundUnboundUnbound
1g7mCUnboundUnbound
UnboundUnboundUnbound
1kipCUnboundUnbound
UnboundUnboundUnbound
1kiqCUnboundUnbound
UnboundUnboundUnbound
1kirCUnboundUnbound
UnboundUnboundUnbound
1melLUnboundUnbound
UnboundUnboundUnbound
1melMUnboundUnbound
UnboundUnboundUnbound
1mlcEUnboundUnbound
UnboundUnboundUnbound
1mlcFUnboundUnbound
UnboundUnboundUnbound
1vfbCUnboundUnbound
UnboundUnboundUnbound
2hflYUnboundUnbound
UnboundUnboundUnbound
2iffYUnboundUnbound
UnboundUnboundUnbound
3hflYUnboundUnbound
UnboundUnboundUnbound
3hfmYUnboundUnbound
UnboundUnboundUnbound
1bqlYUnboundUnbound
UnboundUnboundUnbound
1dkjAUnboundUnbound
UnboundUnboundUnbound
1dkkAUnboundUnbound
UnboundUnboundUnbound
1dkkBUnboundUnbound
UnboundUnboundUnbound
1ghlAUnboundUnbound
UnboundUnboundUnbound
1ghlBUnboundUnbound
UnboundUnboundUnbound
1jhlAUnboundUnbound
UnboundUnboundUnbound
135lAUnboundUnbound
UnboundUnboundUnbound
1dzbXUnboundUnbound
UnboundUnboundUnbound
1dzbYUnboundUnbound
UnboundUnboundUnbound
1jefAUnboundUnbound
UnboundBound:NAG-NAG-NAGUnbound
1jseAUnboundUnbound
UnboundUnboundUnbound
1jtpLUnboundUnbound
UnboundUnboundUnbound
1jtpMUnboundUnbound
UnboundUnboundUnbound
1lz3AUnboundUnbound
UnboundUnboundUnbound
1lzyAUnboundUnbound
UnboundBound:NAG-NAGUnbound
1tewAUnboundUnbound
UnboundUnboundUnbound
2lz2AUnboundUnbound
UnboundUnboundUnbound
3lz2AUnboundUnbound
UnboundUnboundUnbound
1fbiXUnboundUnbound
UnboundUnboundUnbound
1fbiYUnboundUnbound
UnboundUnboundUnbound
1hhlAUnboundUnbound
UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P00698
pdbCatalytic residuescomment
1a2yCGLU 35;ASP 52
mutant D18A
1at5AGLU 35;ASP 52

1at6AGLU 35;ASP 52

1bvkCGLU 35;ASP 52

1bvkFGLU 35;ASP 52

1dqjCGLU 35;ASP 52

1fdlYGLU 35;ASP 52

1g7hCGLU 35;ASP 52

1g7iCGLU 35;ASP 52

1g7jCGLU 35;ASP 52

1g7lCGLU 35;ASP 52

1g7mCGLU 35;ASP 52

1kipCGLU 35;ASP 52

1kiqCGLU 35;ASP 52

1kirCGLU 35;ASP 52

1melLGLU 35;ASP 52

1melMGLU 35;ASP 52

1mlcEGLU 35;ASP 52

1mlcFGLU 35;ASP 52

1vfbCGLU 35;ASP 52

2hflYGLU 35;ASP 52

2iffYGLU 35;ASP 52

3hflYGLU 35;ASP 52

3hfmYGLU 35;ASP 52

1bqlYGLU 35;ASP 52

1dkjAGLU 35;ASP 52

1dkkAGLU 35;ASP 52

1dkkBGLU 35;ASP 52

1ghlAGLU 35;ASP 52

1ghlBGLU 35;ASP 52

1jhlAGLU 35;ASP 52

135lAGLU 35;ASP 52

1dzbXGLU 35;ASP 52

1dzbYGLU 35;ASP 52

1jefAGLU 35;ASP 52

1jseAGLU 35;ASP 52

1jtpLGLU 35;ASP 52

1jtpMGLU 35;ASP 52

1lz3AGLU 35;ASP 52

1lzyAGLU 35;ASP 52

1tewAGLU 35;ASP 52

2lz2AGLU 35;ASP 52

3lz2AGLU 35;ASP 52

1fbiXGLU 35;ASP 52

1fbiYGLU 35;ASP 52

1hhlAGLU 35;ASP 52


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[13]

[27]Fig.12
[40]p.1894-1895
[41]Scheme 1, p.18862
[43]

[49]Fig.4, p.19980-19981
[60]Fig.1
[64]Fig.(5), p.109-1103
[69]Fig.1, Fig.2, p.7383
[70]Figure 1p.835

references
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PubMed ID5891407
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Year1965
Volume206
Pages757-61
AuthorsBlake CC, Koenig DF, Mair GA, North AC, Phillips DC, Sarma VR
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Related Swiss-protP00698
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND REVIEW.
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Year1972
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Pages665-868
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Related Swiss-protP00698
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF TRICLINIC LYSOZYME.
Medline ID76146540
PubMed ID1255720
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Volume101
Pages11-24
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Related Swiss-protP00698
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF TRICLINIC LYSOZYME.
Medline ID76146521
PubMed ID1255711
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Volume100
Pages179-95
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Related Swiss-protP00698
[5]
CommentsSTRUCTURE BY NMR.
Medline ID88163558
PubMed ID3349024
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Year1988
Volume27
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Related Swiss-protP00698
[6]
CommentsX-ray crystallography
PubMed ID2762305
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Related PDB3hfm
[7]
PubMed ID2302221
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Year1990
Volume166
Pages1039-46
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[8]
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[10]
CommentsSTRUCTURE BY NMR.
Medline ID92176179
PubMed ID1794991
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Volume110
Pages997-1003
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Related Swiss-protP00704
[11]
PubMed ID1761525
JournalJ Biochem (Tokyo)
Year1991
Volume110
Pages295-300
AuthorsNakazawa T, Sakiyama F
TitleSite-specific 13C-labeling of Trp 62 in hen egg-white lysozyme: preparation and 13C-NMR titration of [delta 1-13C]Trp 62-lysozyme.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH ANTIBODY.
Medline ID91302305
PubMed ID1712773
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Year1991
Volume266
Pages12915-20
AuthorsFischmann TO, Bentley GA, Bhat TN, Boulot G, Mariuzza RA, Phillips SE, Tello D, Poljak RJ
TitleCrystallographic refinement of the three-dimensional structure of the FabD1.3-lysozyme complex at 2.5-A resolution.
Related PDB1fdl
Related Swiss-protP00698
[13]
PubMed ID1856865
JournalJ Mol Biol
Year1991
Volume220
Pages401-24
AuthorsStrynadka NC, James MN
TitleLysozyme revisited: crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D.
[14]
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Year1992
Volume111
Pages1-3
AuthorsYao M, Tanaka I, Hikichi K, Nitta K
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[15]
PubMed ID1587860
JournalJ Biol Chem
Year1992
Volume267
Pages10842-9
AuthorsWilson KP, Malcolm BA, Matthews BW
TitleStructural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.
[16]
PubMed ID1569548
JournalJ Mol Biol
Year1992
Volume224
Pages613-28
AuthorsCheetham JC, Artymiuk PJ, Phillips DC
TitleRefinement of an enzyme complex with inhibitor bound at partial occupancy. Hen egg-white lysozyme and tri-N-acetylchitotriose at 1.75 A resolution.
[17]
PubMed ID1553384
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Year1992
Volume12
Pages91-9
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[18]
PubMed ID1515108
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Year1992
Volume48
Pages200-7
AuthorsHowell PL, Almo SC, Parsons MR, Hajdu J, Petsko GA
TitleStructure determination of turkey egg-white lysozyme using Laue diffraction data.
Related PDB3lz2
[19]
PubMed ID8422374
JournalBiochemistry
Year1993
Volume32
Pages669-78
AuthorsBuck M, Radford SE, Dobson CM
TitleA partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding.
[20]
PubMed ID8373783
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Year1993
Volume32
Pages9851-8
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[21]
PubMed ID8444153
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Year1993
Volume212
Pages151-6
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[22]
PubMed ID8445657
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Year1993
Volume229
Pages930-44
AuthorsSmith LJ, Sutcliffe MJ, Redfield C, Dobson CM
TitleStructure of hen lysozyme in solution.
[23]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID93361517
PubMed ID8356074
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Year1993
Volume90
Pages7711-5
AuthorsChitarra V, Alzari PM, Bentley GA, Bhat TN, Eisele JL, Houdusse A, Lescar J, Souchon H, Poljak RJ
TitleThree-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex.
Related PDB1ghl,1jhl,1hhl
Related Swiss-protP00702
[24]
PubMed ID8180215
JournalBiochemistry
Year1994
Volume33
Pages5867-76
AuthorsHooke SD, Radford SE, Dobson CM
TitleThe refolding of human lysozyme: a comparison with the structurally homologous hen lysozyme.
[25]
PubMed ID8125914
JournalJ Biol Chem
Year1994
Volume269
Pages7070-5
AuthorsMaenaka K, Kawai G, Watanabe K, Sunada F, Kumagai I
TitleFunctional and structural role of a tryptophan generally observed in protein-carbohydrate interaction. TRP-62 of hen egg white lysozyme.
[26]
CommentsX-ray crystallography
PubMed ID7966295
JournalJ Mol Biol
Year1994
Volume243
Pages767-81
AuthorsBraden BC, Souchon H, Eisele JL, Bentley GA, Bhat TN, Navaza J, Poljak RJ
TitleThree-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1.
Related PDB1mlc
[27]
PubMed ID7966306
JournalJ Mol Biol
Year1994
Volume243
Pages856-72
AuthorsHadfield AT, Harvey DJ, Archer DB, MacKenzie DA, Jeenes DJ, Radford SE, Lowe G, Dobson CM, Johnson LN
TitleCrystal structure of the mutant D52S hen egg white lysozyme with an oligosaccharide product.
[28]
PubMed ID8289250
JournalJ Mol Biol
Year1994
Volume235
Pages302-17
AuthorsYoung AC, Tilton RF, Dewan JC
TitleThermal expansion of hen egg-white lysozyme. Comparison of the 1.9 A resolution structures of the tetragonal form of the enzyme at 100 K and 298 K.
[29]
CommentsX-ray crystallography
PubMed ID8302837
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Year1994
Volume91
Pages1089-93
AuthorsBhat TN, Bentley GA, Boulot G, Greene MI, Tello D, Dall'Acqua W, Souchon H, Schwarz FP, Mariuzza RA, Poljak RJ
TitleBound water molecules and conformational stabilization help mediate an antigen-antibody association.
Related PDB1vfb
[30]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID94339839
PubMed ID8061608
JournalProtein Sci
Year1994
Volume3
Pages788-98
AuthorsLescar J, Souchon H, Alzari PM
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Related Swiss-protP00702,P00704
[31]
PubMed ID7696270
JournalBiochemistry
Year1995
Volume34
Pages4041-55
AuthorsBuck M, Boyd J, Redfield C, MacKenzie DA, Jeenes DJ, Archer DB, Dobson CM
TitleStructural determinants of protein dynamics: analysis of 15N NMR relaxation measurements for main-chain and side-chain nuclei of hen egg white lysozyme.
[32]
PubMed ID7548086
JournalBiochemistry
Year1995
Volume34
Pages13219-32
AuthorsBuck M, Schwalbe H, Dobson CM
TitleCharacterization of conformational preferences in a partly folded protein by heteronuclear NMR spectroscopy: assignment and secondary structure analysis of hen egg-white lysozyme in trifluoroethanol.
[33]
PubMed ID7628485
JournalEur J Biochem
Year1995
Volume231
Pages56-64
AuthorsFukamizo T, Hatta T, Goto S
TitleHen-egg-white lysozyme modified with histamine. State of the imidazolylethyl group covalently attached to the binding site and its effect on the sugar-binding ability.
[34]
CommentsSynchrotron X-ray crystallography
PubMed ID7629116
JournalJ Biol Chem
Year1995
Volume270
Pages18067-76
AuthorsLescar J, Pellegrini M, Souchon H, Tello D, Poljak RJ, Peterson N, Greene M, Alzari PM
TitleCrystal structure of a cross-reaction complex between Fab F9.13.7 and guinea fowl lysozyme.
Related PDB1fbi
[35]
CommentsX-ray crystallography
PubMed ID7531245
JournalJ Mol Biol
Year1995
Volume245
Pages261-74
AuthorsChacko S, Silverton E, Kam-Morgan L, Smith-Gill S, Cohen G, Davies D
TitleStructure of an antibody-lysozyme complex unexpected effect of conservative mutation.
Related PDB2iff,3hfl
[36]
PubMed ID7707375
JournalJ Mol Biol
Year1995
Volume247
Pages281-93
AuthorsMaenaka K, Matsushima M, Song H, Sunada F, Watanabe K, Kumagai I
TitleDissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity.
[37]
PubMed ID8535242
JournalProtein Sci
Year1995
Volume4
Pages2063-72
AuthorsShih P, Kirsch JF
TitleDesign and structural analysis of an engineered thermostable chicken lysozyme.
[38]
CommentsX-ray crystallography
JournalActa Crystallogr D Biol Crystallogr
Year1996
Volume52
Pages315-26
AuthorsCohen GH, Sheriff S, Davies DR
TitleRefined Structure of the Monoclonal Antibody HyHEL-5 with its Antigen Hen Egg-White Lysozyme.
Related PDB3hfl
[39]
CommentsX-ray crystallography
PubMed ID8952503
JournalBiochemistry
Year1996
Volume35
Pages15494-503
AuthorsFields BA, Goldbaum FA, Dall'Acqua W, Malchiodi EL, Cauerhff A, Schwarz FP, Ysern X, Poljak RJ, Mariuzza RA
TitleHydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme.
Related PDB1kip,1kiq,1kir
[40]
PubMed ID8639671
JournalBiochemistry
Year1996
Volume35
Pages1890-6
AuthorsMatsumura I, Kirsch JF
TitleSynergistic contributions of asparagine 46 and aspartate 52 to the catalytic mechanism of chicken egg white lysozyme.
[41]
PubMed ID8639670
JournalBiochemistry
Year1996
Volume35
Pages1881-9
AuthorsMatsumura I, Kirsch JF
TitleIs aspartate 52 essential for catalysis by chicken egg white lysozyme? The role of natural substrate-assisted hydrolysis.
[42]
PubMed ID8807857
JournalChem Biol
Year1996
Volume3
Pages295-9
AuthorsVogel K, Cook J, Chmielewski J
TitleSubtilisin-catalyzed religation of proteolyzed hen egg-white lysozyme: investigation of the role of disulfides.
[43]
PubMed ID8907188
JournalJ Biochem (Tokyo)
Year1996
Volume119
Pages145-50
AuthorsHashimoto Y, Yamada K, Motoshima H, Omura T, Yamada H, Yasukochi T, Miki T, Ueda T, Imoto T
TitleA mutation study of catalytic residue Asp 52 in hen egg lysozyme.
[44]
PubMed ID8780785
JournalJ Mol Biol
Year1996
Volume261
Pages443-53
AuthorsBolin KA, Pitkeathly M, Miranker A, Smith LJ, Dobson CM
TitleInsight into a random coil conformation and an isolated helix: structural and dynamical characterisation of the C-helix peptide from hen lysozyme.
[45]
PubMed ID8632472
JournalJ Mol Biol
Year1996
Volume257
Pages889-94
AuthorsBraden BC, Fields BA, Ysern X, Goldbaum FA, Dall'Acqua W, Schwarz FP, Poljak RJ, Mariuzza RA
TitleCrystal structure of the complex of the variable domain of antibody D1.3 and turkey egg white lysozyme: a novel conformational change in antibody CDR-L3 selects for antigen.
[46]
CommentsX-ray crystallography
PubMed ID8784355
JournalNat Struct Biol
Year1996
Volume3
Pages803-11
AuthorsDesmyter A, Transue TR, Ghahroudi MA, Thi MH, Poortmans F, Hamers R, Muyldermans S, Wyns L
TitleCrystal structure of a camel single-domain VH antibody fragment in complex with lysozyme.
Related PDB1mel
[47]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID97035273
PubMed ID8880929
JournalProteins
Year1996
Volume26
Pages55-65
AuthorsChacko S, Silverton EW, Smith-Gill SJ, Davies DR, Shick KA, Xavier KA, Willson RC, Jeffrey PD, Chang CY, Sieker LC, Sheriff S
TitleRefined structures of bobwhite quail lysozyme uncomplexed and complexed with the HyHEL-5 Fab fragment.
Related PDB1bql,1dkj,1dkk
Related Swiss-protP00700
[48]
CommentsSTRUCTURE BY NMR.
Medline ID97365184
PubMed ID9220986
JournalBiochemistry
Year1997
Volume36
Pages8977-91
AuthorsSchwalbe H, Fiebig KM, Buck M, Jones JA, Grimshaw SB, Spencer A, Glaser SJ, Smith LJ, Dobson CM
TitleStructural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea.
Related Swiss-protP00698
[49]
PubMed ID9242666
JournalJ Biol Chem
Year1997
Volume272
Pages19976-81
AuthorsKuroki R, Ito Y, Kato Y, Imoto T
TitleA covalent enzyme-substrate adduct in a mutant hen egg white lysozyme (D52E).
[50]
PubMed ID9312083
JournalJ Biol Chem
Year1997
Volume272
Pages24843-9
AuthorsRoux P, Delepierre M, Goldberg ME, Chaffotte AF
TitleKinetics of secondary structure recovery during the refolding of reduced hen egg white lysozyme.
[51]
PubMed ID9408946
JournalProteins
Year1997
Volume29
Pages492-507
AuthorsBhattacharjya S, Balaram P
TitleEffects of organic solvents on protein structures: observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide.
[52]
PubMed ID9639564
JournalBiochem J
Year1998
Volume333
Pages71-6
AuthorsMaenaka K, Matsushima M, Kawai G, Kidera A, Watanabe K, Kuroki R, Kumagai I
TitleStructural and functional effect of Trp-62-->Gly and Asp-101-->Gly substitutions on substrate-binding modes of mutant hen egg-white lysozymes.
[53]
CommentsX-ray crystallography
PubMed ID9609690
JournalBiochemistry
Year1998
Volume37
Pages7981-91
AuthorsDall'Acqua W, Goldman ER, Lin W, Teng C, Tsuchiya D, Li H, Ysern X, Braden BC, Li Y, Smith-Gill SJ, Mariuzza RA
TitleA mutational analysis of binding interactions in an antigen-antibody protein-protein complex.
Related PDB1a2y
[54]
PubMed ID9602036
JournalBiochim Biophys Acta
Year1998
Volume1384
Pages23-31
AuthorsMaenaka K, Matsushima M, Kawai G, Watanabe K, Kuroki R, Kumagai I
TitleStructural analysis of mutant hen egg-white lysozyme preferring a minor binding mode.
[55]
CommentsX-ray crystallography
PubMed ID9463398
JournalJ Exp Med
Year1998
Volume187
Pages479-85
AuthorsHolmes MA, Buss TN, Foote J
TitleConformational correction mechanisms aiding antigen recognition by a humanized antibody.
Related PDB1bvk
[56]
PubMed ID9571046
JournalJ Mol Biol
Year1998
Volume278
Pages231-8
AuthorsNoguchi S, Miyawaki K, Satow Y
TitleSuccinimide and isoaspartate residues in the crystal structures of hen egg-white lysozyme complexed with tri-N-acetylchitotriose.
[57]
PubMed ID9517539
JournalProteins
Year1998
Volume30
Pages232-43
AuthorsHarata K, Abe Y, Muraki M
TitleFull-matrix least-squares refinement of lysozymes and analysis of anisotropic thermal motion.
Related PDB1jse
[58]
PubMed ID10469657
JournalEMBO J
Year1999
Volume18
Pages4794-803
Authorsvan den Berg B, Chung EW, Robinson CV, Mateo PL, Dobson CM
TitleThe oxidative refolding of hen lysozyme and its catalysis by protein disulfide isomerase.
[59]
PubMed ID9990012
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages1262-7
AuthorsKnubovets T, Osterhout JJ, Connolly PJ, Klibanov AM
TitleStructure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol.
[60]
PubMed ID10325403
JournalProtein Eng
Year1999
Volume12
Pages327-31
AuthorsIto Y, Kuroki R, Ogata Y, Hashimoto Y, Sugimura K, Imoto T
TitleAnalysis of a catalytic pathway via a covalent adduct of D52E hen egg white mutant lysozyme by further mutation.
[61]
PubMed ID10651280
JournalProteins
Year1999
Volume37
Pages654-67
AuthorsHaliloglu T, Bahar I
TitleStructure-based analysis of protein dynamics: comparison of theoretical results for hen lysozyme with X-ray diffraction and NMR relaxation data.
[62]
CommentsX-ray crystallography
PubMed ID10828942
JournalBiochemistry
Year2000
Volume39
Pages6296-309
AuthorsLi Y, Li H, Smith-Gill SJ, Mariuzza RA
TitleThree-dimensional structures of the free and antigen-bound Fab from monoclonal antilysozyme antibody HyHEL-63(,).
Related PDB1dqj
[63]
CommentsX-ray crystallography
PubMed ID11112523
JournalBiochemistry
Year2000
Volume39
Pages15375-87
AuthorsSundberg EJ, Urrutia M, Braden BC, Isern J, Tsuchiya D, Fields BA, Malchiodi EL, Tormo J, Schwarz FP, Mariuzza RA
TitleEstimation of the hydrophobic effect in an antigen-antibody protein-protein interface.
Related PDB1g7h,1g7i,1g7j,1g7l,1g7m
[64]
PubMed ID12369923
JournalCurr Protein Pept Sci
Year2000
Volume1
Pages105-24
AuthorsFukamizo T
TitleChitinolytic enzymes: catalysis, substrate binding, and their application.
[65]
CommentsX-ray crystallography
PubMed ID10926506
JournalJ Mol Biol
Year2000
Volume301
Pages239-46
AuthorsAy J, Keitel T, Kuttner G, Wessner H, Scholz C, Hahn M, Hohne W
TitleCrystal structure of a phage library-derived single-chain Fv fragment complexed with turkey egg-white lysozyme at 2.0 A resolution.
Related PDB1dzb
[66]
PubMed ID10708653
JournalProtein Eng
Year2000
Volume13
Pages133-41
AuthorsMande SC, Sobhia ME
TitleStructural characterization of protein-denaturant interactions: crystal structures of hen egg-white lysozyme in complex with DMSO and guanidinium chloride.
[67]
PubMed ID11112507
JournalProtein Eng
Year2000
Volume13
Pages691-5
AuthorsMasumoto K, Ueda T, Motoshima H, Imoto T
TitleRelationship between local structure and stability in hen egg white lysozyme mutant with alanine substituted for glycine.
[68]
PubMed ID11718564
JournalJ Mol Biol
Year2001
Volume314
Pages311-20
AuthorsTachibana H, Oka T, Akasaka K
TitleNative-like tertiary structure formation in the alpha-domain of a hen lysozyme two-disulfide variant.
[69]
PubMed ID11524668
JournalNat Struct Biol
Year2001
Volume8
Pages737-9
AuthorsKirby AJ
TitleThe lysozyme mechanism sorted -- after 50 years.
[70]
PubMed ID11518970
JournalNature
Year2001
Volume412
Pages835-8
AuthorsVocadlo DJ, Davies GJ, Laine R, Withers SG
TitleCatalysis by hen egg-white lysozyme proceeds via a covalent intermediate.
[71]
PubMed ID11274458
JournalProtein Sci
Year2001
Volume10
Pages677-88
AuthorsSchwalbe H, Grimshaw SB, Spencer A, Buck M, Boyd J, Dobson CM, Redfield C, Smith LJ
TitleA refined solution structure of hen lysozyme determined using residual dipolar coupling data.
[72]
PubMed ID11093257
JournalProteins
Year2001
Volume42
Pages17-22
AuthorsXue Y, Liu JN, Sun Z, Ma Z, Wu C, Zhu D
Titlealpha-lactalbumin mutant acting as lysozyme.
[73]
PubMed ID11676532
JournalJ Mol Biol
Year2001
Volume313
Pages473-8
AuthorsDecanniere K, Transue TR, Desmyter A, Maes D, Muyldermans S, Wyns L
TitleDegenerate interfaces in antigen-antibody complexes.
Related PDB1jtp
[74]
PubMed ID11841203
JournalBiochemistry
Year2002
Volume41
Pages2130-9
AuthorsNoda Y, Yokota A, Horii D, Tominaga T, Tanisaka Y, Tachibana H, Segawa S
TitleNMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.
[75]
PubMed ID12654268
JournalJ Mol Biol
Year2003
Volume327
Pages857-65
AuthorsRefaee M, Tezuka T, Akasaka K, Williamson MP
TitlePressure-dependent changes in the solution structure of hen egg-white lysozyme.

comments
This enzyme belongs to the glycosidase family-22. This is a retaining enzyme, which hydrolyzes beta-(1-4)-glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine (GlcNAc).
Although earlier study (see [27]) proposed that Asp52 acts as a stabilizer, which stabilizes the oxocarbenium ion intermediate, recent papers confirmed that Asp52 acts as a nucleophile that will form a covalent intermediate with C1 atom of the sugar substrate (see [69] & [70]). Meanwhile, Glu35 acts as an acid-base catalyst.
Thus, according to the literature [69] & [70], the catalytic reaction proceeds with a concerted SN2-type reaction as follows:
(1) Glu35 acts as a general acid, to protonate the glycosidic oxygen of the scissile bond, whilst asp52 makes a nucleophilic attack on the C1 atom of the GlcNAc, to form a covalent intermediate with it. This reaction leads to the bond cleavage between the glycosidic linkage.
(2) Glu35 acts as a general base, which activates a water molecule. The activated water makes a nucleophilic attack on the C1 atom, to hydrolyze the intermediate.

createdupdated
2004-03-032009-02-26


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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