KEGG   ENZYME: 3.4.21.10Help
Entry
EC 3.4.21.10                Enzyme                                 

Name
acrosin;
acrosomal proteinase;
acrozonase;
alpha-acrosin;
beta-acrosin;
upsilon-acrosin;
acrosomal protease;
acrosin amidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Serine endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Preferential cleavage: Arg!, Lys!
Comment
Occurs in spermatozoa; formed from proacrosin by limited proteolysis. Inhibited by naturally occurring trypsin inhibitors. In peptidase family S1 (trypsin family)
History
EC 3.4.21.10 created 1972
Orthology
K01317  acrosin
Genes
HSA: 49(ACR)
PTR: 458950(ACR)
PPS: 100979160(ACR)
GGO: 101144239(ACR)
PON: 100448292(ACR)
NLE: 100586140(ACR)
MCC: 716579(ACR)
MCF: 102115325(ACR)
CSAB: 103223579 103223651(ACR)
RRO: 104655563(ACR)
RBB: 108545017(ACR)
CJC: 100406660(ACR)
SBQ: 101047167(ACR)
MMU: 11434(Acr)
RNO: 24163(Acr)
CGE: 100754856(Acr)
NGI: 103735496(Acr)
HGL: 101712354(Acr)
CCAN: 109693070(Acr)
OCU: 100009184(ACR)
TUP: 102477933(ACR)
CFA: 606765(ACR)
AML: 100482745(ACR)
UMR: 103674103(ACR)
ORO: 101363888 101379789(ACR)
FCA: 101083949(ACR)
PTG: 102954045(ACR)
AJU: 106987633(ACR)
BTA: 280711(ACR)
BOM: 102270129(ACR)
PHD: 102317784(ACR)
CHX: 102191416(ACR)
OAS: 443195(ACR)
SSC: 397098(ACR)
CFR: 102504353(ACR)
CDK: 105106149(ACR)
BACU: 103017313(ACR)
LVE: 103072664(ACR)
OOR: 101282422(ACR)
ECB: 100057028(ACR)
EPZ: 103543987(ACR)
EAI: 106846026(ACR)
MYB: 102256900(ACR)
MYD: 102774021(ACR)
HAI: 109396613(ACR)
PALE: 102886339(ACR)
LAV: 100674496(ACR)
TMU: 101350147
MDO: 103093639
GGA: 426864(ACR)
MGP: 100539639 692129(ACR)
ACYG: 106029620 106048161(ACR)
FPG: 101920858
EGZ: 104122507
AAM: 106496144
CMY: 102938123(Acrosin) 102938344(Acrosin)
GJA: 107118562(ACR) 107120174
NPR: 108802724
LCM: 102354559
CMK: 103180626 103190823(acr)
 » show all
Taxonomy
Reference
1  [PMID:7043204]
  Authors
Muller-Esterl W, Fritz H.
  Title
Sperm Acrosin.
  Journal
Methods Enzymol 80 Pt C:621-32 (1981)
Reference
2  [PMID:2500154]
  Authors
Skoog MT, Mehdi S, Wiseman JS, Bey P.
  Title
The specificity of two proteinases that cleave adjacent to arginine, C1 esterase and acrosin, for peptide p-nitroanilide substrates.
  Journal
Biochim Biophys Acta 996:89-94 (1989)
DOI:10.1016/0167-4838(89)90099-X
Reference
3  [PMID:2114285]
  Authors
Keime S, Adham IM, Engel W.
  Title
Nucleotide sequence and exon-intron organization of the human proacrosin gene.
  Journal
Eur J Biochem 190:195-200 (1990)
DOI:10.1111/j.1432-1033.1990.tb15564.x
  Sequence
[hsa:49]
Other DBs
ExplorEnz - The Enzyme Database: 3.4.21.10
IUBMB Enzyme Nomenclature: 3.4.21.10
ExPASy - ENZYME nomenclature database: 3.4.21.10
BRENDA, the Enzyme Database: 3.4.21.10
CAS: 9068-57-9

DBGET integrated database retrieval system