EzCatDB: D00430
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DB codeD00430
RLCP classification1.13.30000.10 : Hydrolysis
CATH domainDomain 12.40.10.10 : Thrombin, subunit HCatalytic domain
Domain 22.40.10.10 : Thrombin, subunit HCatalytic domain
E.C.3.4.21.50

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,D00426,M00133,D00428,D00429,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
UniProtKBKEGG

P15636
Protein nameProtease 1lysyl endopeptidase
Achromobacter proteinase I (also see Comment)
Achromobacter lyticus alkaline proteinase I
protease I
achromopeptidase
lysyl bond specific proteinase
SynonymsEC 3.4.21.50
Protease I
API
Lysyl endopeptidase
MEROPSS01.280 (Serine)
PfamPF01483 (P_proprotein)
PF00801 (PKD)
[Graphical view]


UniProtKB:Accession NumberP15636
Entry nameAPI_ACHLY
ActivityPreferential cleavage: Lys-|-Xaa, including Lys-|-Pro.
Subunit
Subcellular locationSecreted.
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00017C00012C00001C00017C00012I00087I00085I00086
CompoundProteinPeptideH2OProteinPeptidePeptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinpeptide/proteinH2Opeptide/proteinpeptide/protein


ChEBI

15377





PubChem

962
22247451





                
1arbA01UnboundUnbound UnboundUnbound   
1arcA01UnboundAnalogue:TCK UnboundUnbound   
1arbA02UnboundUnbound UnboundUnbound   
1arcA02UnboundUnbound UnboundUnbound   

Active-site residues
resource
Swiss-prot;P15636 & literature[2]
pdbCatalytic residuesMain-chain involved in catalysis
          
1arbA01SER 194
GLY 192;SER 194
1arcA01SER 194
GLY 192;SER 194
1arbA02HIS 57;ASP 113
 
1arcA02HIS 57;ASP 113
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.6, p.4157

references
[1]
CommentsX-ray crystallography
PubMed ID2492988
JournalJ Biol Chem
Year1989
Volume264
Pages3832-9
AuthorsTsunasawa S, Masaki T, Hirose M, Soejima M, Sakiyama F
TitleThe primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease.
Related PDB1arb,1arc
[2]
PubMed ID7845202
JournalMethods Enzymol
Year1994
Volume244
Pages126-37
AuthorsSakiyama F, Masaki T
TitleLysyl endopeptidase of Achromobacter lyticus.
[3]
PubMed ID12180992
JournalEur J Biochem
Year2002
Volume269
Pages4152-8
AuthorsShiraki K, Norioka S, Li S, Yokota K, Sakiyama F
TitleElectrostatic role of aromatic ring stacking in the pH-sensitive modulation of a chymotrypsin-type serine protease, Achromobacter protease I.
[4]
PubMed ID11820934
JournalJ Biochem (Tokyo)
Year2002
Volume131
Pages213-8
AuthorsShiraki K, Norioka S, Li S, Sakiyama F
TitleContribution of an imidazole-indole stack to high catalytic potency of a lysine-specific serine protease, Achromobacter protease I.

comments
This enzyme belongs to the peptidase family-S5.
According to the papers [2], [3] & [4], this enzyme has got a similar catalytic triad to that of trypsin, suggesting a similar catalytic mechanism.

createdupdated
2004-04-272011-02-18


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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)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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