DB code: T00410

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
-.-.-.- :
E.C. 3.4.21.10
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
2.40.10.10 : Thrombin, subunit H M00139 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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains MEROPS Pfam RefSeq
Q9GL10 Acrosin
EC 3.4.21.10
Acrosin light chain
Acrosin heavy chain
S01.223 (Serine)
PF00089 (Trypsin)
[Graphical View]
P08001 Acrosin
EC 3.4.21.10
53 kDa fucose-binding protein
Acrosin light chain
Acrosin heavy chain
S01.223 (Serine)
PF00089 (Trypsin)
[Graphical View]
NP_999198.1 (Protein)
NM_214033.1 (DNA/RNA sequence)

KEGG enzyme name
Acrosin
Acrosomal proteinase
Acrozonase
Alpha-acrosin
Beta-acrosin
Upsilon-acrosin
Acrosomal protease
Acrosin amidase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P08001 ACRO_PIG Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. Heavy chain (catalytic) and a light chain linked by two disulfide bonds.
Q9GL10 ACRO_SHEEP Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. Heavy chain (catalytic) and a light chain linked by two disulfide bonds.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00012 C00001 C00012 C03253 I00087 I00085 I00086
E.C.
Compound Peptide H2O Peptide Amino acid(Arg-, Lys-) Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type peptide/protein H2O peptide/protein amino acids,amine group
ChEBI 15377
PubChem 22247451
962
1fiwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fizA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fiwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fizA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fiwL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1fizL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Literature [2] & Swiss-prot;Q9GL10, P08001

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1fiwA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1fizA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1fiwA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;ASP 194;SER 195
1fizA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;ASP 194;SER 195
1fiwL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1fizL Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Figure 5

References
[1]
Resource
Comments
Medline ID
PubMed ID 8737992
Journal Biol Chem Hoppe Seyler
Year 1996
Volume 377
Pages 261-5
Authors Adham IM, Kremling H, Nieter S, Zimmermann S, Hummel M, Schroeter U, Engel W
Title The structures of the bovine and porcine proacrosin genes and their conservation among mammals.
Related PDB
Related UniProtKB
[2]
Resource
Comments NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 18-329.
Medline ID
PubMed ID 11080640
Journal Structure
Year 2000
Volume 8
Pages 1179-88
Authors Tranter R, Read JA, Jones R, Brady RL
Title Effector sites in the three-dimensional structure of mammalian sperm beta-acrosin.
Related PDB 1fiw 1fiz
Related UniProtKB Q9GL10 P08001
[3]
Resource
Comments
Medline ID
PubMed ID 12475199
Journal Chem Rev
Year 2002
Volume 102
Pages 4501-24
Authors Hedstrom L
Title Serine protease mechanism and specificity.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 12012776
Journal Zoolog Sci
Year 2002
Volume 19
Pages 139-51
Authors Sawada H
Title Ascidian sperm lysin system.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 18649284
Journal Int J Dev Biol
Year 2008
Volume 52
Pages 717-36
Authors Topfer-Petersen E, Ekhlasi-Hundrieser M, Tsolova M
Title Glycobiology of fertilization in the pig.
Related PDB
Related UniProtKB

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.

Created Updated
2011-02-04 2011-09-14