EzCatDB: M00167

DB codeM00167
RLCP classification1.13.30000.10
CATH domainDomain 13.30.300.50
Domain 23.30.300.50
Domain 32.40.10.10Catalytic domain
Domain 42.40.10.10Catalytic domain
E.C.3.4.21.12
CSA2lpr

CATH domainRelated DB codes (homologues)
2.40.10.10M00139,D00214,D00426,M00133,D00428,D00429,D00430,D00431,D00432,D00433,D00434,D00435,M00227,M00209,D00194,D00197,D00211,D00212,D00216,M00212,D00224,D00497,M00217,M00216,D00528,D00848,D00850,D00851,D00852,D00855,M00152,M00155,M00157,M00181,M00315,M00316,M00317,M00348,M00349,T00074,T00410,T00411

Enzyme Name
Swiss-protKEGG

P00778
Protein nameAlpha-lytic proteasealpha-lytic endopeptidase
myxobacter alpha-lytic proteinase
alpha-lytic proteinase
alpha-lytic protease
Mycobacterium sorangium alpha-lytic proteinase
Myxobacter 495 alpha-lytic proteinase
alpha-lytic proteinase
Myxobacter alpha-lytic proteinase
Mycobacterium sorangium alpha-lytic proteinase
SynonymsEC 3.4.21.12
Alpha-lytic endopeptidase


Swiss-prot:Accession NumberP00778
Entry namePRLA_LYSEN
ActivityPreferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins.
Subunit
Subcellular location
Cofactor


SubstratesProductsintermediates
KEGG-idC00012C02065C00001C00012C00098I00087I00085I00086
CompoundPeptideProtein alanineH2OPeptideOligopeptidePeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinamine group,carboxyl group,peptide/protein


2proA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2proB01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2proC01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3proC01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3proD01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
4proC01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
4proD01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2proA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2proB02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2proC02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3proC02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3proD02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
4proC02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
4proD02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1boqA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbaA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbbA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbcA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbdA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbeA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbfA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbhA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbiA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbjA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbkA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gblA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbmA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p01A01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p02A01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p03A01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p04A01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p05A01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p06A01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p09A01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p10A01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p11E01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p12E01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1qq4A01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1qrwA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1qrxA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1talA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2alpA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2lprA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2ullA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3lprA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3proA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3proB01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
4proA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
4proB01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
5lprA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
6lprA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
7lprA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
8lprA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
9lprA01UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1boqA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbaA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbbA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2A(chain P)
1gbcA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-BLE(chain P)
1gbdA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2F(chain P)
1gbeA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbfA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2A(chain P)
1gbhA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-BLE(chain P)
1gbiA02UnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:ALA-ALA-PRO-B2F(chain P)Unbound
1gbjA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1gbkA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2A(chain P)
1gblA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-BLE(chain P)
1gbmA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2F(chain P)
1p01A02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:BOC-ALA-PRO-B2V(chain P)
1p02A02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2A(chain P)
1p03A02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2V(chain P)
1p04A02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2I(chain P)
1p05A02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-BNO(chain P)
1p06A02UnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:ALA-ALA-PRO-B2F(chain P)Unbound
1p09A02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1p10A02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2V(chain P)
1p11E02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:BOC-ALA-ALA-PRO-PVA-LAC-ALA(chain P),BOC-ALA-ALA-PRO-PVA(chain I)
1p12E02UnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:BOC-ALA-ALA-PRO-PVA-LAC-ALA(chain I)Unbound
1qq4A02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1qrwA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1qrxA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
1talA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2alpA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
2lprA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2V(chain P)
2ullA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
3lprA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-BNO(chain P)
3proA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:2AB
3proB02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:2AB
4proA02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
4proB02UnboundUnbound
UnboundUnboundUnboundUnboundUnbound
5lprA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2A(chain P)
6lprA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-BNO(chain P)
7lprA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-BLE(chain P)
8lprA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-B2F(chain P)
9lprA02UnboundUnbound
UnboundUnboundUnboundUnboundTransition-state-analogue:ALA-ALA-PRO-BLE(chain P)

Active-site residues
resource
Swiss-prot;P00778
pdbCatalytic residuesMain-chain involved in catalysiscomment
2proA01


2proB01


2proC01


3proC01


3proD01


4proC01


4proD01


2proA02


2proB02


2proC02


3proC02


3proD02


4proC02


4proD02


1boqA01HIS 36;ASP  63


1gbaA01HIS 57;ASP 102


1gbbA01HIS 57;ASP 102


1gbcA01HIS 57;ASP 102


1gbdA01HIS 57;ASP 102


1gbeA01HIS 57;ASP 102


1gbfA01HIS 57;ASP 102


1gbhA01HIS 57;ASP 102


1gbiA01HIS 57;ASP 102


1gbjA01HIS 57;ASP 102


1gbkA01HIS 57;ASP 102


1gblA01HIS 57;ASP 102


1gbmA01HIS 57;ASP 102


1p01A01HIS 57;ASP 102


1p02A01HIS 57;ASP 102


1p03A01HIS 57;ASP 102


1p04A01HIS 57;ASP 102


1p05A01HIS 57;ASP 102


1p06A01HIS 57;ASP 102


1p09A01HIS 57;ASP 102


1p10A01HIS 57;ASP 102


1p11E01HIS 57;ASP 102


1p12E01HIS 57;ASP 102


1qq4A01HIS 36;ASP  63


1qrwA01HIS 36;ASP  63


1qrxA01HIS 36;ASP  63


1talA01HIS 57;ASP 102


2alpA01HIS 57;ASP 102


2lprA01HIS 57;ASP 102


2ullA01HIS 57;ASP 102


3lprA01HIS 57;ASP 102


3proA01HIS 36;ASP  63


3proB01HIS 36;ASP  63


4proA01HIS 36;ASP  63


4proB01HIS 36;ASP  63


5lprA01HIS 57;ASP 102


6lprA01HIS 57;ASP 102


7lprA01HIS 57;ASP 102


8lprA01HIS 57;ASP 102


9lprA01HIS 57;ASP 102


1boqA02SER 143
GLY 141;SER 143

1gbaA02SER 195
GLY 193;SER 195
mutant M190A, G216A
1gbbA02SER 195
GLY 193;SER 195
mutant M190A, G216A
1gbcA02SER 195
GLY 193;SER 195
mutant M190A, G216A
1gbdA02SER 195
GLY 193;SER 195
mutant M190A, G216A
1gbeA02SER 195
GLY 193;SER 195
mutant M190A, G216L
1gbfA02SER 195
GLY 193;SER 195
mutant M190A, G216L
1gbhA02SER 195
GLY 193;SER 195
mutant M190A, G216L
1gbiA02SER 195
GLY 193;SER 195
mutant M190A, G216L
1gbjA02SER 195
GLY 193;SER 195
mutant M190A
1gbkA02SER 195
GLY 193;SER 195
mutant M190A
1gblA02SER 195
GLY 193;SER 195
mutant M190A
1gbmA02SER 195
GLY 193;SER 195
mutant M190A
1p01A02SER 195
GLY 193;SER 195

1p02A02SER 195
GLY 193;SER 195

1p03A02SER 195
GLY 193;SER 195

1p04A02SER 195
GLY 193;SER 195

1p05A02SER 195
GLY 193;SER 195

1p06A02SER 195
GLY 193;SER 195

1p09A02SER 195
GLY 193;SER 195
mutant M213A
1p10A02SER 195
GLY 193;SER 195
mutant M213A
1p11E02SER 195
GLY 193;SER 195

1p12E02SER 195
GLY 193;SER 195

1qq4A02SER 143
GLY 141;SER 143
mutant R102H, G134S
1qrwA02SER 143
GLY 141;SER 143
mutant R102H, G134S
1qrxA02SER 143
GLY 141;SER 143

1talA02SER 195
GLY 193;SER 195

2alpA02SER 195
GLY 193;SER 195

2lprA02SER 195
GLY 193;SER 195
mutant M192A
2ullA02SER 195
GLY 193;SER 195

3lprA02SER 195
GLY 193;SER 195
mutant M192A
3proA02SER 143
GLY 141;SER 143
mutant M158A
3proB02SER 143
GLY 141;SER 143
mutant M158A
4proA02SER 143
GLY 141;SER 143
mutant M158A
4proB02SER 143
GLY 141;SER 143
mutant M158A
5lprA02SER 195
GLY 193;SER 195
mutant M213A
6lprA02SER 195
GLY 193;SER 195
mutant M213A
7lprA02SER 195
GLY 193;SER 195
mutant M213A
8lprA02SER 195
GLY 193;SER 195
mutant M213A
9lprA02SER 195
GLY 193;SER 195


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]equation (1), equation (2), equation (3), equation (4), p.768-771
[4]Fig.1, p.424-428
[9]Fig.6, p.7613-7614
[10]p.7695-7696
[37]Fig.3, p.10374-10376

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed ID117110
JournalJ Mol Biol
Year1979
Volume131
Pages743-75
AuthorsBrayer GD, Delbaere LT, James MN
TitleMolecular structure of the alpha-lytic protease from Myxobacter 495 at 2.8 Angstroms resolution.
Related Swiss-protP00778
[2]
PubMed ID6769571
JournalCan J Biochem
Year1980
Volume58
Pages252-71.
AuthorsJames MN
TitleAn X-ray crystallographic approach to enzyme structure and function.
[3]
PubMed ID7038675
JournalProc Natl Acad Sci U S A
Year1981
Volume78
Pages7323-6
AuthorsBachovchin WW, Kaiser R, Richards JH, Roberts JD
TitleCatalytic mechanism of serine proteases: reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease.
[4]
PubMed ID7049067
JournalAnnu Rev Biophys Bioeng
Year1982
Volume11
Pages419-44
AuthorsSteitz TA, Shulman RG
TitleCrystallographic and NMR studies of the serine proteases.
[5]
PubMed ID6802183
JournalBiochim Biophys Acta
Year1982
Volume702
Pages105-11
AuthorsRecchia J, Matthews CR, Rhee MJ, Horrocks WD Jr
TitleInterresidue distance measurements in proteins. Fluorescent energy transfer between tryptophans and a Ru(III)(NH3)5-histidine complex in alpha-lytic protease and lysozyme.
[6]
PubMed ID6395886
JournalBiochemistry
Year1984
Volume23
Pages5933-7
AuthorsHuang TH, Bachovchin WW, Griffin RG, Dobson CM
TitleHigh-resolution nitrogen-15 nuclear magnetic resonance studies of alpha-lytic protease in solid state. Direct comparison of enzyme structure in solution and in the solid state.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed ID3900416
JournalJ Mol Biol
Year1985
Volume184
Pages479-502
AuthorsFujinaga M, Delbaere LT, Brayer GD, James MN
TitleRefined structure of alpha-lytic protease at 1.7 A resolution. Analysis of hydrogen bonding and solvent structure.
Related PDB2alp
Related Swiss-protP00778
[8]
PubMed ID3934665
JournalProc Natl Acad Sci U S A
Year1985
Volume82
Pages7948-51
AuthorsBachovchin WW
TitleConfirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme.
[9]
CommentsX-ray crystallography
PubMed ID3122831
JournalBiochemistry
Year1987
Volume26
Pages7609-14
AuthorsBone R, Shenvi AB, Kettner CA, Agard DA
TitleSerine protease mechanism: structure of an inhibitory complex of alpha-lytic protease and a tightly bound peptide boronic acid.
Related PDB1p01
[10]
PubMed ID3207700
JournalBiochemistry
Year1988
Volume27
Pages7689-97
AuthorsBachovchin WW, Wong WY, Farr-Jones S, Shenvi AB, Kettner CA
TitleNitrogen-15 NMR spectroscopy of the catalytic-triad histidine of a serine protease in peptide boronic acid inhibitor complexes.
[11]
CommentsX-ray crystallography
PubMed ID2611204
JournalBiochemistry
Year1989
Volume28
Pages7600-9
AuthorsBone R, Frank D, Kettner CA, Agard DA
TitleStructural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates.
Related PDB1p02,1p03,1p04,1p05,1p06
[12]
PubMed ID2646278
JournalJ Bacteriol
Year1989
Volume171
Pages1320-5
AuthorsSilen JL, Frank D, Fujishige A, Bone R, Agard DA
TitleAnalysis of prepro-alpha-lytic protease expression in Escherichia coli reveals that the pro region is required for activity.
[13]
CommentsX-ray crystallography
PubMed ID2716847
JournalNature
Year1989
Volume339
Pages191-5
AuthorsBone R, Silen JL, Agard DA
TitleStructural plasticity broadens the specificity of an engineered protease.
Related PDB1p09,1p10
[14]
PubMed ID2223778
JournalBiochemistry
Year1990
Volume29
Pages7468-74
AuthorsBrothers HM 2nd, Kostic NM
TitleCatalytic activity of the serine proteases alpha-chymotrypsin and alpha-lytic protease tagged at the active site with a (terpyridine)platinum(II) chromophore.
[15]
CommentsX-ray crystallography
PubMed ID1931963
JournalBiochemistry
Year1991
Volume30
Pages10388-98
AuthorsBone R, Fujishige A, Kettner CA, Agard DA
TitleStructural basis for broad specificity in alpha-lytic protease mutants.
Related PDB2lpr,3lpr,5lpr,6lpr,7lpr,8lpr,9lpr
[16]
CommentsX-ray crystallography
PubMed ID1998685
JournalBiochemistry
Year1991
Volume30
Pages2263-72
AuthorsBone R, Sampson NS, Bartlett PA, Agard DA
TitleCrystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters.
Related PDB1p11,1p12
[17]
PubMed ID1856870
JournalJ Mol Biol
Year1991
Volume220
Pages495-506
AuthorsWilson C, Mace JE, Agard DA
TitleComputational method for the design of enzymes with altered substrate specificity.
[18]
PubMed ID1896427
JournalProteins
Year1991
Volume10
Pages140-8
AuthorsCaldwell JW, Agard DA, Kollman PA
TitleFree energy calculations on binding and catalysis by alpha-lytic protease: the role of substrate size in the P1 pocket.
[19]
PubMed ID1445861
JournalBiochemistry
Year1992
Volume31
Pages11216-23
AuthorsEpstein DM, Abeles RH
TitleRole of serine 214 and tyrosine 171, components of the S2 subsite of alpha-lytic protease, in catalysis.
[20]
PubMed ID8251483
JournalBiochemistry
Year1993
Volume32
Pages12651-5
AuthorsTsilikounas E, Kettner CA, Bachovchin WW
Title11B NMR spectroscopy of peptide boronic acid inhibitor complexes of alpha-lytic protease. Direct evidence for tetrahedral boron in both boron-histidine and boron-serine adduct complexes.
[21]
PubMed ID8445659
JournalJ Mol Biol
Year1993
Volume229
Pages996-1006
AuthorsWilson C, Gregoret LM, Agard DA
TitleModeling side-chain conformation for homologous proteins using an energy-based rotamer search.
[22]
PubMed ID7944385
JournalArch Biochem Biophys
Year1994
Volume314
Pages132-41
AuthorsHaggett KD, Graham LD, Milner SJ, Whittaker RG
TitlePurification and characterization of S1 mutants of alpha-lytic protease having altered catalytic properties.
[23]
PubMed ID8155642
JournalBiochemistry
Year1994
Volume33
Pages4251-7
AuthorsSchellenberger V, Turck CW, Rutter WJ
TitleRole of the S' subsites in serine protease catalysis. Active-site mapping of rat chymotrypsin, rat trypsin, alpha-lytic protease, and cercarial protease from Schistosoma mansoni.
[24]
CommentsX-ray crystallography
PubMed ID7500345
JournalJ Mol Biol
Year1995
Volume254
Pages720-36
AuthorsMace JE, Agard DA
TitleKinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity.
Related PDB1gba,1gbb,1gbc,1gbd,1gbe,1gbf,1gbh,1gbi,1gbj,1gbk,1gbl,1gbm
[25]
PubMed ID7643381
JournalJ Mol Biol
Year1995
Volume251
Pages116-34
AuthorsMace JE, Wilk BJ, Agard DA
TitleFunctional linkage between the active site of alpha-lytic protease and distant regions of structure: scanning alanine mutagenesis of a surface loop affects activity and substrate specificity.
[26]
PubMed ID9092819
JournalBiochemistry
Year1997
Volume36
Pages3894-902
AuthorsSohl JL, Shiau AK, Rader SD, Wilk BJ, Agard DA
TitleInhibition of alpha-lytic protease by pro region C-terminal steric occlusion of the active site.
[27]
PubMed ID9335113
JournalJ Biomol NMR
Year1997
Volume10
Pages21-7
AuthorsDavis JH, Agard DA, Handel TM, Basus VJ
TitleAlterations in chemical shifts and exchange broadening upon peptide boronic acid inhibitor binding to alpha-lytic protease.
[28]
CommentsX-ray crystallography
PubMed ID9232638
JournalProtein Sci
Year1997
Volume6
Pages1375-86
AuthorsRader SD, Agard DA
TitleConformational substates in enzyme mechanism: the 120 K structure of alpha-lytic protease at 1.5 A resolution.
Related PDB1tal,2ull
[29]
PubMed ID9353195
JournalScience
Year1997
Volume278
Pages1128-32
AuthorsAsh EL, Sudmeier JL, De Fabo EC, Bachovchin WW
TitleA low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment.
[30]
PubMed ID9601029
JournalBiochemistry
Year1998
Volume37
Pages7696-707
AuthorsDavis JH, Agard DA
TitleRelationship between enzyme specificity and the backbone dynamics of free and inhibited alpha-lytic protease.
[31]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed ID9724517
JournalBiochemistry
Year1998
Volume37
Pages12058-67
AuthorsPeters RJ, Shiau AK, Sohl JL, Anderson DE, Tang G, Silen JL, Agard DA
TitlePro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease.
Related PDB1boq
Related Swiss-protP00778
[32]
CommentsX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed ID9808037
JournalNat Struct Biol
Year1998
Volume5
Pages945-50
AuthorsSauter NK, Mau T, Rader SD, Agard DA
TitleStructure of alpha-lytic protease complexed with its pro region.
Related PDB2pro,3pro,4pro
Related Swiss-protP00778
[33]
PubMed ID9796818
JournalNature
Year1998
Volume395
Pages817-9
AuthorsSohl JL, Jaswal SS, Agard DA
TitleUnfolded conformations of alpha-lytic protease are more stable than its native state.
[34]
PubMed ID9931265
JournalJ Mol Biol
Year1999
Volume286
Pages267-78
AuthorsMiller DW, Agard DA
TitleEnzyme specificity under dynamic control: a normal mode analysis of alpha-lytic protease.
[35]
PubMed ID10500115
JournalProc Natl Acad Sci U S A
Year1999
Volume96
Pages11008-14
AuthorsCunningham EL, Jaswal SS, Sohl JL, Agard DA
TitleKinetic stability as a mechanism for protease longevity.
[36]
PubMed ID10802737
JournalNat Struct Biol
Year2000
Volume7
Pages394-7
AuthorsDerman AI, Agard DA
TitleTwo energetically disparate folding pathways of alpha-lytic protease share a single transition state.
[37]
PubMed ID10984533
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages10371-6
AuthorsAsh EL, Sudmeier JL, Day RM, Vincent M, Torchilin EV, Haddad KC, Bradshaw EM, Sanford DG, Bachovchin WW
TitleUnusual 1H NMR chemical shifts support (His) Cepsilon 1.O==C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis.
[38]
PubMed ID10944390
JournalProteins
Year2000
Volume41
Pages21-32
AuthorsInuzuka Y, Lazaridis T
TitleOn the unfolding of alpha-lytic protease and the role of the pro region.
[39]
PubMed ID11420442
JournalProtein Sci
Year2001
Volume10
Pages1403-14
AuthorsOta N, Agard DA
TitleEnzyme specificity under dynamic control II: Principal component analysis of alpha-lytic protease using global and local solvent boundary conditions.
[40]
PubMed ID12102628
JournalBiochemistry
Year2002
Volume41
Pages8860-7
AuthorsCunningham EL, Mau T, Truhlar SM, Agard DA
TitleThe pro region N-terminal domain provides specific interactions required for catalysis of alpha-lytic protease folding.
[41]
PubMed ID11814352
JournalBiochemistry
Year2002
Volume41
Pages1587-90
AuthorsIvanov D, Bachovchin WW, Redfield AG
TitleBoron-11 pure quadrupole resonance investigation of peptide boronic acid inhibitors bound to alpha-lytic protease.
[42]
PubMed ID11797014
JournalNature
Year2002
Volume415
Pages343-6
AuthorsJaswal SS, Sohl JL, Davis JH, Agard DA
TitleEnergetic landscape of alpha-lytic protease optimizes longevity through kinetic stability.
[43]
PubMed ID14609332
JournalBiochemistry
Year2003
Volume42
Pages13212-9
AuthorsCunningham EL, Agard DA
TitleInterdependent folding of the N- and C-terminal domains defines the cooperative folding of alpha-lytic protease.
[44]
PubMed ID14504841
JournalEur Biophys J
Year2004
Volume33
Pages83-8
AuthorsCabrita LD, Bottomley SP
TitleHow do proteins avoid becoming too stable? Biophysical studies into metastable proteins.
[45]
PubMed ID15111063
JournalJ Mol Biol
Year2004
Volume338
Pages999-1013
AuthorsFuhrmann CN, Kelch BA, Ota N, Agard DA
TitleThe 0.83 A resolution crystal structure of alpha-lytic protease reveals the detailed structure of the active site and identifies a source of conformational strain.
[46]
PubMed ID14739318
JournalProtein Sci
Year2004
Volume13
Pages325-31
AuthorsCunningham EL, Agard DA
TitleDisabling the folding catalyst is the last critical step in alpha-lytic protease folding.

comments
This enzyme belongs to the peptidase family-S1E.
According to the literature [4] & [37], this enzyme has got a catalytic triad, composed of Ser/His/Asp, with a similar catalytic mechanism to that of trypsin (D00197 in EzCatDB).

createdupdated
2004-11-182011-02-23
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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