EzCatDB: T00410
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DB codeT00410
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
Domain 3-.-.-.-
E.C.3.4.21.10

CATH domainRelated DB codes (homologues)
2.40.10.10 : Thrombin, subunit HM00139,D00214,M00167,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,T00411

Enzyme Name
UniProtKBKEGG

Q9GL10P08001
Protein nameAcrosinAcrosinAcrosin
Acrosomal proteinase
Acrozonase
Alpha-acrosin
Beta-acrosin
Upsilon-acrosin
Acrosomal protease
Acrosin amidase
SynonymsEC 3.4.21.10
EC 3.4.21.10
53 kDa fucose-binding protein
ContainsAcrosin light chain
Acrosin heavy chain
Acrosin light chain
Acrosin heavy chain
RefSeq
NP_999198.1 (Protein)
NM_214033.1 (DNA/RNA sequence)
MEROPSS01.223 (Serine)
S01.223 (Serine)
PfamPF00089 (Trypsin)
[Graphical view]
PF00089 (Trypsin)
[Graphical view]


UniProtKB:Accession NumberQ9GL10P08001
Entry nameACRO_SHEEPACRO_PIG
ActivityPreferential cleavage: Arg-|-Xaa, Lys-|-Xaa.Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
SubunitHeavy chain (catalytic) and a light chain linked by two disulfide bonds.Heavy chain (catalytic) and a light chain linked by two disulfide bonds.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idC00012C00001C00012C03253I00087I00085I00086
CompoundPeptideH2OPeptideAmino acid(Arg-, Lys-)Peptidyl-tetrahedral intermediateAcyl-enzymeTetrahedral intermediate
Typepeptide/proteinH2Opeptide/proteinamino acids,amine group


ChEBI
15377





PubChem
962
22247451





               
1fiwA01Unbound UnboundUnboundUnboundUnboundUnbound
1fizA01Unbound UnboundUnboundUnboundUnboundUnbound
1fiwA02Unbound UnboundUnboundUnboundUnboundUnbound
1fizA02Unbound UnboundUnboundUnboundUnboundUnbound
1fiwLUnbound UnboundUnboundUnboundUnboundUnbound
1fizLUnbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Literature [2] & Swiss-prot;Q9GL10, P08001
pdbCatalytic residuesMain-chain involved in catalysis
          
1fiwA01HIS 57;ASP 102
 
1fizA01HIS 57;ASP 102
 
1fiwA02SER 195
GLY 193;ASP 194;SER 195
1fizA02SER 195
GLY 193;ASP 194;SER 195
1fiwL 
 
1fizL 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Figure 5

references
[1]
PubMed ID8737992
JournalBiol Chem Hoppe Seyler
Year1996
Volume377
Pages261-5
AuthorsAdham IM, Kremling H, Nieter S, Zimmermann S, Hummel M, Schroeter U, Engel W
TitleThe structures of the bovine and porcine proacrosin genes and their conservation among mammals.
[2]
CommentsNUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 18-329.
PubMed ID11080640
JournalStructure
Year2000
Volume8
Pages1179-88
AuthorsTranter R, Read JA, Jones R, Brady RL
TitleEffector sites in the three-dimensional structure of mammalian sperm beta-acrosin.
Related PDB1fiw,1fiz
Related UniProtKBQ9GL10,P08001
[3]
PubMed ID12475199
JournalChem Rev
Year2002
Volume102
Pages4501-24
AuthorsHedstrom L
TitleSerine protease mechanism and specificity.
[4]
PubMed ID12012776
JournalZoolog Sci
Year2002
Volume19
Pages139-51
AuthorsSawada H
TitleAscidian sperm lysin system.
[5]
PubMed ID18649284
JournalInt J Dev Biol
Year2008
Volume52
Pages717-36
AuthorsTopfer-Petersen E, Ekhlasi-Hundrieser M, Tsolova M
TitleGlycobiology of fertilization in the pig.

comments
This enzyme belongs to the peptidase family-S1.
This protein is composed of a non-catalytic heavy chain and a catalytic light chain. These two chains are linked by a disulfide bond (see [2]).
According to the literature [2], this enzyme has got the catalytic triad, which is a signature of serine proteases; His57, Asp102 and Ser195. Thus, this enzyme catalyze the same reaction as trypsin family enzymes.

createdupdated
2011-02-042011-09-14


Copyright: Nozomi Nagano, JST & CBRC-AIST
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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 2008)
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)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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