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
Q9GL10	ACRO_SHEEP	Preferential cleavage: Arg-\|-Xaa, Lys-\|-Xaa.	Heavy chain (catalytic) and a light chain linked by two disulfide bonds.
P08001	ACRO_PIG	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 15377
PubChem		22247451 962 22247451 962

1fiwA01	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
1fizA01	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
1fiwA02	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
1fizA02	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
1fiwL	Unbound		Unbound	Unbound	Unbound	Unbound	Unbound
1fizL	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	HIS 57;ASP 102
1fizA01	HIS 57;ASP 102
1fiwA02	SER 195			GLY 193;ASP 194;SER 195
1fizA02	SER 195			GLY 193;ASP 194;SER 195
1fiwL
1fizL

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.

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