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Information on EC 3.4.21.10 - acrosin
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3.4.21.10 acrosinSpecify your search results
Word Map
- 3.4.21.10
- spermatozoa
- semen
- boar
- pellucida
- ejaculate
-
seminal
- infertility
-
capacitation
- oocyte
- epididymal
-
trypsin-like
- gamete
-
bull
-
contraceptive
- ram
-
spermatid
- zymogen
-
spermatogenesis
- hyaluronidase
-
cryopreserved
- benzamidine
-
antifertility
-
autoactivation
- cauda
-
sperm-zona
- kallikreins
-
acrosome-reacted
-
gelatinolytic
-
insemination
-
sperm-associated
- asthenozoospermia
-
andrology
-
sperm-oocyte
-
nonoxynol-9
-
acrosome-intact
-
sperm-egg
- p-aminobenzamidine
-
zona-free
- analysis
-
spermatogonial
-
bapna
- medicine
- tlck
-
kazal-type
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
acrosin, sperm acrosin, beta-acrosin, alpha-acrosin, acrosomal proteinase, acrosomal protease, acrosin amidase, acrosin ii, psi-acrosin, acrosin i, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
53 kDa fucose-binding protein
-
-
-
-
acrosin
acrosin amidase
acrosomal protease
-
-
-
-
acrosomal proteinase
-
-
-
-
acrozonase
-
-
-
-
alpha-acrosin
-
-
-
-
beta-acrosin
proteinase, acrosomal
-
-
-
-
psi-acrosin
-
-
-
-
sperm acrosin
acrosin amidase
-
-
-
-
beta-acrosin
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential cleavage: Arg-/-, Lys-/-
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
9068-57-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aminobenzoyl-Ser-Lys-Gly-Arg-Ser-Leu-Ile-Gly-Lys(dinitrophenyl)-Asp + H2O
?
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
Nalpha-benzoyl-DL-arginyl-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
-
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
-
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proteinase-activated receptor-2 + H2O
?
-
the enzyme may play additional role(s) in the fertilization process via the activation of PAR-2 on oocytes
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
possibly important for fertilization process, involved in the acrosome reaction, binding of spermatozoa to and penetration through the zona pellucida
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
proacrosin involved in stereospecific sulfate binding that mediates the retention of post-acrosome reaction spermatozoa on the zona pellucida surface
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
proteinase-activated receptor-2 + H2O
?
-
the enzyme may play additional role(s) in the fertilization process via the activation of PAR-2 on oocytes
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
-
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
-
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
possibly important for fertilization process, involved in the acrosome reaction, binding of spermatozoa to and penetration through the zona pellucida
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
proacrosin involved in stereospecific sulfate binding that mediates the retention of post-acrosome reaction spermatozoa on the zona pellucida surface
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(3-(2-hydroxyethyl)ureido)-N-(2-methoxybenzyl)-1H-benzo[d]imidazole-5-sulfonamide
-
-
2-(3-(2-hydroxyethyl)ureido)-N-(2-methylbenzyl)-1H-benzo[d]imidazole-5-sulfonamide
-
-
2-{[(2-hydroxyethyl)carbamoyl]amino}-N-[(2-methoxyphenyl)methyl]-1H-benzimidazole-5-sulfonamide
-
-
3-(2,4-dichlorophenyl)isoxazole-5-carbaldehyde
-
50% inhibition at 5.8 mM, weak antifungal activity against Candida albicans
3-(2-bromophenyl)isoxazole-5-carbaldehyde
-
50% inhibition at 1.25 mM, weak antifungal activity against Candida albicans
3-(2-chlorophenyl)isoxazole-5-carbaldehyde
-
50% inhibition at 1.1 mM, weak antifungal activity against Candida albicans
3-(3-bromophenyl)isoxazole-5-carbaldehyde
-
50% inhibition at 4.8 mM, weak antifungal activity against Candida albicans
3-(3-chlorophenyl)isoxazole-5-carbaldehyde
-
50% inhibition at 0.625 mM, weak antifungal activity against Candida albicans
3-(4-chlorophenyl)isoxazole-5-carbaldehyde
-
50% inhibition at 1.8 mM, weak antifungal activity against Candida albicans
3-(4-fluorophenyl)isoxazole-5-carbaldehyde
-
50% inhibition at 4.0 mM, weak antifungal activity against Candida albicans
3-(4-nitrophenyl)isoxazole-5-carbaldehyde
-
50% inhibition at 0.42 mM, weak antifungal activity against Candida albicans
3-methylbutyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
4-carbomethoxyphenyl 4-guanidinobenzoate mesylate
-
4'-CMGB, a sperm acrosin inhibitor and candidate for an vaginal contraceptive drug. Method development and evaluation of 4'-CMGB identification and activity determination involving HPLC and LC-tandem mass spectrometry, overview
5-(2,4-dichlorophenyl)isoxazole-3-carbaldehyde
-
50% inhibition at 0.39 mM, weak antifungal activity against Candida albicans
5-(2-chlorophenyl)isoxazole-3-carbaldehyde
-
50% inhibition at 1.0 mM, weak antifungal activity against Candida albicans
5-(3-bromophenyl)isoxazole-3-carbaldehyde
-
50% inhibition at 1.1 mM, weak antifungal activity against Candida albicans
5-(4-carbamimidamidophenyl)-N-(1-hydroxypropan-2-yl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2,3-dimethylphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2,4-dimethoxyphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2,5-dimethoxyphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2,6-dimethylphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(3,5-dimethylphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(4-methylpyridin-2-yl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-[4-(trifluoromethyl)phenyl]-1,2-oxazole-3-carboxamide hydrochloride
-
-
5-(4-methylphenyl)isoxazole-3-carbaldehyde
-
50% inhibition at 2.4 mM, weak antifungal activity against Candida albicans
5-phenylisoxazole-3-carbaldehyde
-
50% inhibition at 2.4 mM, weak antifungal activity against Candida albicans
Benzamidine hydrochloride
-
50% inhibition at 2.2 mM, weak antifungal activity against Candida albicans
butyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
ethyl 1-[(2,4-dichlorophenyl)acetyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2,4-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2,4-dimethoxyphenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2,6-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-bromo-4-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-chloro-4-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
most potent inhibitor
ethyl 1-[(3,4-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
ethyl 4-([[5-(4-carbamimidamidophenyl)-1,2-oxazol-3-yl]carbonyl]amino)benzoate hydrochloride
-
-
ethyl 5-(4-[[(2,4-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(2,6-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(2,6-difluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(2-bromophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(2-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(4-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(4-fluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(4-methoxyphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(4-methylphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[4-(1-phenylpropyl)benzoyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-([4-[(4-methylphenyl)sulfonyl]benzoyl]amino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-([[4-(chloromethyl)phenyl]carbonyl]amino)phenyl]-1H-pyrazole-3-carboxylate
-
-
methyl (6-[[4-(trifluoromethyl)phenyl]sulfamoyl]-1H-benzimidazol-2-yl)carbamate
-
-
methyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
methyl 4-methyl-3-([4-[(2-methylbenzyl)(methylsulfonyl)amino]benzoyl]amino)benzoate
-
-
N-(2-chlorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-(2-fluorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-(3, 5-difluorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-(3,5-dichlorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-(3-bromophenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
N-(4-chlorophenyl)-N-[2-[(2E)-2-(3-methoxy-4-methylbenzylidene)hydrazinyl]-2-oxoethyl]benzenesulfonamide (non-preferred name)
-
-
N-(4-tert-butylphenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
N-[4-[(4-benzylpiperazin-1-yl)carbonyl]phenyl]-2,3,5,6-tetramethylbenzenesulfonamide
-
-
N-[4-[(4-benzylpiperazin-1-yl)carbonyl]phenyl]-4-tert-butylbenzenesulfonamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylpiperidin-1-yl)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylpiperidin-1-yl)acetamide
-
-
propan-2-yl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
propyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
seminal plasma acrosin inhibitor
-
a member of the Kazal-type subfamily from the boar reproductive tract, expression and localization in the epithelium and lumen of cauda epididymidis, seminal vesicles, prostate, and Cowper's glands, overview
-
suramin
-
compound with combined antifertility agent and microbicide, three to four molecules of suramin bind to one molecule of enzyme
suramin
-
compound with combined antifertility agent and microbicide, three to four molecules of suramin bind to one molecule of enzyme
additional information
-
inhibited by naturally occuring trypsin inhibitors, esterolytic activity, competitively inhibited by L-arginine but not by L-lysine
-
additional information
-
inhibited by naturally occuring trypsin inhibitors, esterolytic activity, competitively inhibited by L-arginine but not by L-lysine; nearly all trypsin inhibitors
-
additional information
-
inhibited by naturally occuring trypsin inhibitors, esterolytic activity, competitively inhibited by L-arginine but not by L-lysine
-
additional information
-
inhibited by naturally occuring trypsin inhibitors, esterolytic activity, competitively inhibited by L-arginine but not by L-lysine
-
additional information
-
no inhibition with quercetin-3beta-D-glucoside or quercetin-3beta-D-glucoside sulfate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-methylarachidonoyl-2'-fluoro-ethylamide
-
i.e. MET-F-AEA, significantly increases at 10 nM, whereas higher MET-F-AEA levels do not induce the enzymatic activity.10 nM MET-F-AEA combined with 0.001 mM selective CB1-receptor antagonist SR141716 significantly increases the acrosin activity, while 0.001 mM CB2-receptor antagonist, SR144528 plus 10 nM MET-F-AEA and 0.001 mM capsazapine plus 10 nM METF-AEA have a similar behavior to that observed by using 10 nM MET-F-AEA alone
lysophosphatidylcholine
-
in heparin-capacitated spermatozoa, the addition of lysophosphatidylcholine produces a significant increase (about 7fold) in acrosin activity
additional information
-
activated by 2-methylpropan-2-ol, dimethyl sulfoxide and some other water-miscible solvents
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.022
aminobenzoyl-Ser-Lys-Gly-Arg-Ser-Leu-Ile-Gly-Lys(dinitrophenyl)-Asp
-
pH 7.4, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
320
aminobenzoyl-Ser-Lys-Gly-Arg-Ser-Leu-Ile-Gly-Lys(dinitrophenyl)-Asp
-
pH 7.4, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.78
1-(2,4-dichlorobenzoyl)-N-methyl-1H-indazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00563
2,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00596
2,6-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
6.04
2-(3-(2-hydroxyethyl)ureido)-N-(2-methoxybenzyl)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
5.45
2-(3-(2-hydroxyethyl)ureido)-N-(2-methylbenzyl)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00935
2-(4-chlorophenoxy)-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00763
2-bromo-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0063
2-chloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
7.32
2-{[(2-hydroxyethyl)carbamoyl]amino}-N-[(2-methoxyphenyl)methyl]-1H-benzimidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0038
3,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.42
3-(4-nitrophenyl)-1,2-oxazole-5-carbaldehyde
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.007
3-chloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00251
3-methylbutyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0033
3-[4-([[4-(aminomethyl)cyclohexyl]carbonyl]oxy)phenyl]propanoic acid
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.008
4-(acetylamino)phenyl 4-carbamimidamidobenzoate
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.00384
4-(chloromethyl)-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00925
4-([4-[3-(ethoxycarbonyl)-1H-pyrazol-5-yl]phenyl]amino)-4-oxobutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.3447
4-[(2-methylbenzyl)(methylsulfonyl)amino]-N-(pyridin-4-ylmethyl)benzamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.1
5-(4-carbamimidamidophenyl)-N-(1-hydroxypropan-2-yl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0115
5-(4-carbamimidamidophenyl)-N-(2,3-dimethylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0014
5-(4-carbamimidamidophenyl)-N-(2,4-dimethoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0023
5-(4-carbamimidamidophenyl)-N-(2,5-dimethoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0057
5-(4-carbamimidamidophenyl)-N-(2,6-dimethylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0084
5-(4-carbamimidamidophenyl)-N-(2-methoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0144
5-(4-carbamimidamidophenyl)-N-(2-methylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0121
5-(4-carbamimidamidophenyl)-N-(3,5-dimethylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0254
5-(4-carbamimidamidophenyl)-N-(3-chlorophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0066
5-(4-carbamimidamidophenyl)-N-(3-methoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0094
5-(4-carbamimidamidophenyl)-N-(3-methylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0268
5-(4-carbamimidamidophenyl)-N-(4-chlorophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0239
5-(4-carbamimidamidophenyl)-N-(4-cyanophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0064
5-(4-carbamimidamidophenyl)-N-(4-ethoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0205
5-(4-carbamimidamidophenyl)-N-(4-fluorophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0101
5-(4-carbamimidamidophenyl)-N-(4-methylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0214
5-(4-carbamimidamidophenyl)-N-(4-methylpyridin-2-yl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0299
5-(4-carbamimidamidophenyl)-N-(naphthalen-1-yl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.1
5-(4-carbamimidamidophenyl)-N-(propan-2-yl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0246
5-(4-carbamimidamidophenyl)-N-phenyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
0.0203
5-(4-carbamimidamidophenyl)-N-[4-(trifluoromethyl)phenyl]-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8°C
0.0174
5-([4-[3-(ethoxycarbonyl)-1H-pyrazol-5-yl]phenyl]amino)-5-oxopentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0095
butyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
3.24
ethyl 1-(2,4-dichlorobenzoyl)-1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00221
ethyl 1-(phenylcarbonyl)-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00029
ethyl 1-[(2,4-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00174
ethyl 1-[(2-bromo-4-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00347
ethyl 1-[(2-chloro-4-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00299
ethyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0093
ethyl 4-([[5-(4-carbamimidamidophenyl)-1,2-oxazol-3-yl]carbonyl]amino)benzoate hydrochloride
Homo sapiens
-
pH 7.8, 37.8°C
0.00044
ethyl 5-(4-[[(2,4-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0048
ethyl 5-(4-[[(2,6-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00398
ethyl 5-(4-[[(2,6-difluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0024
ethyl 5-(4-[[(2-bromophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
ethyl 5-(4-[[(2-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00331
ethyl 5-(4-[[(4-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0024
ethyl 5-(4-[[(4-fluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
ethyl 5-(4-[[(4-methoxyphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0346
ethyl 5-(4-[[(4-methylphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0033
ethyl 5-(4-[[4-(1-phenylpropyl)benzoyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.023
ethyl 5-[4-(acetylamino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.46
ethyl 5-[4-(benzoylamino)phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8°C
0.017
ethyl 5-[4-(butanoylamino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.072
ethyl 5-[4-(pentanoylamino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.014
ethyl 5-[4-(propanoylamino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000032
ethyl 5-[4-([4-[(4-methylphenyl)sulfonyl]benzoyl]amino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00331
ethyl 5-[4-([[4-(chloromethyl)phenyl]carbonyl]amino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.06
ethyl 5-[4-[(2-chlorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8°C
0.24
ethyl 5-[4-[(3,4-dichlorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8°C
0.00576
ethyl 5-[4-[(3-chloropropanoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00047
ethyl 5-[4-[(4-benzylbenzoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.38
ethyl 5-[4-[(4-chlorobenzoyl)amino]phenyl]1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8°C
0.14
ethyl 5-[4-[(4-fluorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8°C
0.008
ethyl 5-[4-[(phenylcarbonyl)amino]phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0079
ethyl 5-[4-[(trifluoroacetyl)amino]phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
10.7
methyl (6-[[4-(trifluoromethyl)phenyl]sulfamoyl]-1H-benzimidazol-2-yl)carbamate
Homo sapiens
-
pH 8.0, 22°C
0.0093
methyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.1555
methyl 4-methyl-3-([4-[(2-methylbenzyl)(methylsulfonyl)amino]benzoyl]amino)benzoate
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.47
methyl [6-(propan-2-ylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
1.27
methyl [6-[(2,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
1.55
methyl [6-[(2,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
8.86
methyl [6-[(2,5-dimethylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
5.75
methyl [6-[(2-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
0.31
methyl [6-[(2-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
8.42
methyl [6-[(2-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
4.02
methyl [6-[(3,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
1.59
methyl [6-[(3,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
11.5
methyl [6-[(3,4-dimethoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
1.81
methyl [6-[(3-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
7.5
methyl [6-[(3-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
5.06
methyl [6-[(3-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
1.64
methyl [6-[(4-bromophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
7.52
methyl [6-[(4-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
2.4
methyl [6-[(4-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
3.29
methyl [6-[(4-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
3.18
methyl [6-[(4-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
1.25
methyl [6-[benzyl(methyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
0.063
methyl [6-[bis(3-methylbutyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22°C
5.73
N,N-bis(2-hydroxyethyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.4267
N,N-dibenzyl-2-[4-(propan-2-ylsulfamoyl)phenoxy]acetamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.0279
N-(2-bromophenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8°C
1.06
N-(2-chlorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.08
N-(2-fluorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
6.81
N-(2-hydroxyethyl)-5-(4-methoxyphenyl)-N-methyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
8.92
N-(2-hydroxypropyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.34
N-(3, 5-difluorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
2.45
N-(3,5-dichlorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0144
N-(3-bromophenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8°C
1.43
N-(3-hydroxypropyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.014
N-(4-chlorophenyl)-N-[2-[(2E)-2-(3-methoxy-4-methylbenzylidene)hydrazinyl]-2-oxoethyl]benzenesulfonamide (non-preferred name)
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.0078
N-(4-tert-butylphenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8°C
5.08
N-(5-bromobenzo[d]thiazol-2-yl)-2-(4-pentylpiperazin-1-yl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
1.09
N-(5-bromobenzo[d]thiazol-2-yl)-2-(diisopentylamino)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.54
N-(5-bromobenzo[d]thiazol-2-yl)-2-(dipentylamino)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
2.78
N-(6-bromobenzo[d]thiazol-2-yl)-2-(dibutylamino)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
142.6
N-alpha-tosyl-L-lysyl-chloromethyl-ketone
Homo sapiens
-
pH and temperature not specified in the publication
0.28
N-benzyl-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.3551
N-cyclohexyl-2-[(4,6-diphenylpyrimidin-2-yl)sulfanyl]acetamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
1.62
N-hexyl-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.1426
N-tosyl-L-lysine chloromethylketone
Homo sapiens
-
pH and temperature not specified in the publication
0.3018
N-[4-(dipropylsulfamoyl)phenyl]-3,4-diethoxybenzamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.6248
N-[4-[(4-benzylpiperazin-1-yl)carbonyl]phenyl]-2,3,5,6-tetramethylbenzenesulfonamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
3.057
N-[4-[(4-benzylpiperazin-1-yl)carbonyl]phenyl]-4-tert-butylbenzenesulfonamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.2053
N-[4-[(4-fluorophenyl)sulfamoyl]phenyl]-3,4,5-trimethoxybenzamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.6678
N-[4-[(4-methoxyphenyl)sulfamoyl]phenyl]-2-(naphthalen-1-yloxy)acetamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.00245
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2,4,6-trimethylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00718
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2,6-difluorobenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0093
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylphenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0099
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylpiperidin-1-yl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00892
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(3-methylphenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00984
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methoxyphenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00898
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylphenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00498
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylpiperidin-1-yl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0042
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-nitrophenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00741
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(piperidin-1-yl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0023
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-phenoxyacetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0025
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3,5-dinitrobenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00705
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3-(trifluoromethyl)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00013
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethoxybenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00021
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00711
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-fluorobenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00221
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methoxybenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00206
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00958
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00158
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]pentanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.009
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]propanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00235
propan-2-yl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00331
propyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.39
5-(2,4-dichlorophenyl)-1,2-oxazole-3-carbaldehyde
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
0.1426
N-alpha-tosyl-L-lysyl-chloromethylketone
Homo sapiens
-
pH and temperature not specified in the publication
0.1426
N-alpha-tosyl-L-lysyl-chloromethylketone
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10.5
-
pH 6.0: about 20% of maximal activity, pH 10.5: about 25% of maximal activity
6.5 - 9.5
-
pH 6.5: about 50% of maximal activity, pH 9.5: about 25% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fragment; East African long-eared elephant shrew
SwissProt
brenda
-
36461, 36462, 36468, 36474, 36479, 36483, 36484, 668680, 668887, 692404, 692405, 707132, 709265, 717353, 717359, 717498, 717912, 731432, 731451, 731747, 753777, 755363
-
-
brenda
infertile and fertile Nigerian men, fertile men are found to have higher acrosin activity in spermatozoa than infertile men, lower enzyme activity is found to correlate with increased morphological changes in the spermatozoa
-
-
brenda
patients with unexplained infertility and infertile males with low motility of semen
-
-
brenda
male
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
brenda
-
compared to control, enzyme activity is significantly lower in patients with unexplained infertility but high sperm mobility and in patients with infertility and low sperm mobility
brenda
-
the protein is distributed on the surface and in the acrosomal matrix of the sperm head
brenda
-
ultrastructure of sterlet sperm, sperm cells possess a head with a distinct acrosome, a midpiece and a single flagellum surrounded by the flagellar plasma membrane, overview. The enzyme is localized in acrosome, endonuclear canals and implantation fossa
brenda
-
ultrastructure of sterlet sperm, sperm cells possess a head with a distinct acrosome, a midpiece and a single flagellum surrounded by the flagellar plasma membrane, overview. The enzyme is localized in acrosome, endonuclear canals and implantation fossa
-
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
-
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
-
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
-
acrosin is expressed in the testis, where it is stored in the acrosomal cap of sperm in its inactive form, proacrosin
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
enzyme subcellular localization analysis, overview
-
brenda
additional information
-
enzyme subcellular localization analysis, overview
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
acrosin is responsible for the serine protease activity associated with the inner acrosomal membrane
physiological function
physiological function
-
sperm acrosin is responsible for the sperm binding to the egg envelope (perivitelline membrane) during fertilization
physiological function
-
acrosin cooperates with matrix metallo-proteinase 2 in sperm penetration of the zona pellucida during fertilization
physiological function
-
the enzyme is capable of hydrolysing the zona pellucida in bovine oocytes
Show AA Sequence and Transmembrane Helices (167 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26300
x * 26300, calculated from the deduced amino acid sequence
27000
30000
30138
x * 30138, calculated from the deduced amino acid sequence
30469
x * 30469, calculated from the deduced amino acid sequence
30534
x * 30534, calculated from the deduced amino acid sequence
30583
30604
x * 30604, calculated from the deduced amino acid sequence
30616
x * 30616, calculated from the deduced amino acid sequence
30628
x * 30628, calculated from the deduced amino acid sequence
32000
-
x * 40000, proacrosin, SDS-PAGE, x * 32000, alpha-acrosin, SDS-PAGE, x * 27000, beta-acrosin, SDS-PAGE
34000
-
x * 52000, x * 68000, x * 34000, SDS-PAGE, 3 forms with different molecular weight
360517
x * 360517, mature protein, calculated from amino acid sequence
38000
40000
41000
46422
x * 46422, calculated from the deduced amino acid sequence
52000
-
x * 52000, x * 68000, x * 34000, SDS-PAGE, 3 forms with different molecular weight
68000
-
x * 52000, x * 68000, x * 34000, SDS-PAGE, 3 forms with different molecular weight
27000
-
x * 40000, proacrosin, SDS-PAGE, x * 32000, alpha-acrosin, SDS-PAGE, x * 27000, beta-acrosin, SDS-PAGE
40000
-
x * 40000, proacrosin, SDS-PAGE, x * 32000, alpha-acrosin, SDS-PAGE, x * 27000, beta-acrosin, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 40000, proacrosin, SDS-PAGE, x * 32000, alpha-acrosin, SDS-PAGE, x * 27000, beta-acrosin, SDS-PAGE
?
x * 30628, calculated from the deduced amino acid sequence
?
-
x * 52000, x * 68000, x * 34000, SDS-PAGE, 3 forms with different molecular weight
additional information
-
interaction of protein with zona pellucida glycoproteins, highest binding activity toward glycoprotein ZPA
additional information
-
proenzyme binds to bovine serum albumin-mannose, binding sites are stabilized by noncovalent bonds and disulfide linkages
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
side-chain modification
glycoprotein
one potential N-glycosylation site is present at Asn-128 and three potential O-glycosylation sites are present at Thr-184, Thr-300 and Thr-312
proteolytic modification
-
96% of acrosin of capacitated sperm samples and control is present in the zymogen form
proteolytic modification
-
acrosin is an acrosomal protease synthesized as an inactive precursor, proacrosin, which is processed via autoproteolysis into active forms alpha- and beta-acrosin, which occurs earlier in frozen/thawed dog spermatozoa than in fresh dog spermatozoa
proteolytic modification
-
the inactive form proacrosin needs to be activated to acrosin autocatalytically during the acrosome reaction
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals grown in the presence of 10 mM 4-aminobenzamidine by vapor diffusion, complex of the enzyme with 4-aminobenzamidine, crystal structure solved to 2.1 and 2.9 A resolution
crystals grown in the presence of 10 mM 4-aminobenzamidine by vapor diffusion, complex of the enzyme with 4-aminobenzamidine, crystal structure solved to 2.1 and 2.9 A resolution
crystals grown in the presence of 10 mM 4-aminobenzamidine by vapor diffusion, complex of the enzyme with 4-aminobenzamidine, crystal structure solved to 2.1 and 2.9 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
bacterial recombinant human proacrosin/acrosin proteins: Rec-40, residues 1-402, Rec-30, N-terminal fragments 1-300, Rec-20, 1-190, and Rec-10, 1-160
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes
no differences are found in the enzyme activity of sperm suspension in fresh and frozen-thawed semen
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
BioSep-SEC-S2000 column chromatography, BioBasic 8 column chromatography, and Superdex 200 gel filtration
-
BioSep-SEC-S2000 gel filtration, BioBasic 8 column chromatography, and Superdex 200 gel filtration
-
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mitochondrial membrane potential dissipation induced by 0.01 mM carbonyl cyanide 3-chlorophenylhydrazone causes significant declines in acrosin activity
-
there is significantly higher acrosin activity in subjects with moderate or high mitochondrial membrane potential compared to those with low mitochondrial membrane potential
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme activity can be used as a reliable predictor of boar sperm freezability
medicine
medicine
-
acrosin activity positively correlates with normal sperm morphology and with fertilization rate. Use of enzyme assay to predict sperm fertilizing capacity in in vitro fertilization independently of sperm morphology
medicine
-
egg-sperm interaction: proenzyme binds to bovine serum albumin-mannose, binding sites are stabilized by noncovalent bonds and disulfide linkages. Binding sites are located both at the N- and C-terminus of protein
medicine
-
sperm-egg interaction: interaction of protein with zona pellucida glycoproteins, highest binding activity with glycoprotein ZPA. Interaction involves mannosyl, fucosyl, and sulfated glycans. Binding sites are located both on N- and C-terminus of proacrosin, revealing a key role of proenzyme in the interaction
medicine
-
use of total enzyme activity as biochemical marker for clinical evaluation of unexplained infertility in males
medicine
-
acrosin represents a potential target for the design and development of male contraceptive agents
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mueller-Esterl, W.; Fritz, H.
Sperm acrosin
Methods Enzymol.
80
621-632
1981
Sus scrofa
brenda
Mukerji, S.K.
Studies on the rabbit proacrosin-acrosin system
Arch. Biochem. Biophys.
230
412-423
1984
Oryctolagus cuniculus
brenda
Zelezna, B.; Cechova, D.
Boar acrosin. Isolation of two active forms from boar ejaculated sperm
Hoppe-Seyler's Z. Physiol. Chem.
363
757-766
1982
Sus scrofa
brenda
Elce, J.S.; McIntyre, E.J.
Purification of bovine and human acrosin
Can. J. Biochem.
60
8-14
1981
Bos taurus, Homo sapiens
brenda
Anderson, R.A.; Beyler, S.A.; Mack, S.R.; Zaneveld, L.J.D.
Characterization of a high-molecular-weight form of human acrosin. Comparison with human pancreatic trypsin
Biochem. J.
199
307-316
1981
Homo sapiens
brenda
Mueller-Esterl, W.; Kupfer, S.; Fritz, H.
Purification and properties of boar acrosin
Hoppe-Seyler's Z. Physiol. Chem.
361
1811-1821
1980
Sus scrofa
brenda
Brown, C.R.; Hartree, E.F.
Studies on ram acrosin. Activation of proacrosin accompanying the isolation of acrosin from spermatozoa, and purification of the enzyme by affinity chromatography
Biochem. J.
175
227-238
1978
Ovis aries
brenda
Schleuning, W.D.; Fritz, H.
Sperm acrosin
Methods Enzymol.
45
330-342
1976
Sus scrofa
brenda
Brown, C.R.; Andani, Z.; Hartree, E.F.
Studies on ram acrosin. Isolation from spermatozoa, activation by cations and organic solvents, and influence of cations on its reaction with inhibitors
Biochem. J.
149
133-146
1975
Ovis aries
brenda
Schleuning, W.D.; Fritz, H.
Some characteristics of highly purified boar sperm acrosin
Hoppe-Seyler's Z. Physiol. Chem.
355
125-130
1974
Sus scrofa
brenda
Gilboa, E.; Elkana, Y.; Rigbi, M.
Purification and properties of human acrosin
Eur. J. Biochem.
39
85-92
1973
Homo sapiens
brenda
Polakoski, K.L.; McRorie, R.A.; Williams, W.L.
Boar acrosin. I. Purification and preliminary characterization of a proteinase from boar sperm acrosomes
J. Biol. Chem.
248
8178-8182
1973
Sus scrofa
brenda
Polakoski, K.L.; McRorie, R.A.
Boar acrosin. II. Classification, inhibition, and specificity studies of a proteinase from sperm acrosomes
J. Biol. Chem.
248
8183-8188
1973
Sus scrofa
brenda
Hardy, D.M.; Schoots, A.F.M.; Hedrick, J.L.
Caprine acrosin. Purification, characterization and proteolysis of the porcine zona pellucida
Biochem. J.
257
447-453
1989
Capra hircus
brenda
Schiessler, H.; Fritz, H.; Arnold, M.; Fink, E.; Tschesche, H.
Properties of the trypsin-like (acrosin) from boar spermatozoa
Hoppe-Seyler's Z. Physiol. Chem.
353
1638-1645
1972
Sus scrofa
brenda
Ho, J.J.L.; Meizel, S.
Multiple molecular forms of avian acrosin: differences in their kinetic properties
FEBS Lett.
56
115-119
1975
Gallus gallus
brenda
Fritz, H.; Foerg-Brey, B.; Meier, M.; Arnold, M.; Tschesche, H.
Human acrosin: inhibition by protein-proteinase inhibitors
Hoppe-Seyler's Z. Physiol. Chem.
353
1950-1952
1972
Homo sapiens
brenda
Uhlenbruck, G.; Sprenger, I.; Schumacher, G.F.B.; Zaneveld, L.J.D.
Additional properties of acrosin, a proteolytic enzyme from rabbit sperm acrosomes
Naturwissenschaften
59
124-125
1972
Oryctolagus cuniculus
brenda
Planchenault, T.; Cechova, D.; Keil-Dlouha, V.
Matrix degrading properties of sperm serine proteinase, acrosin
FEBS Lett.
294
279-281
1991
Sus scrofa
brenda
Hermans, J.M.; Monard, D.; Jones, R.; Stone, S.R.
Inhibition of acrosin by serpins. A suicide substrate mechanism
Biochemistry
34
3678-3685
1995
Sus scrofa
brenda
Falase, E.A.O.; Adekunle, A.O.; Neblett, H.; Teuscher, C.
Guinea pig testicular proacrosin-acrosin system: preliminary immunological characterization
J. Reprod. Immunol.
15
241-256
1989
Cavia porcellus
brenda
Kobayashi, T.; Matsuda, Y.; Oshio, S.; Kaneko, S.; Nozawa, S; Mhori, H.; Akihama, S.; Fujimoto, Y.
Human acrosin: purification and some properties
Arch. Androl.
27
9-16
1991
Homo sapiens
brenda
Takano, H.; Yanagimachi, R.; Urch, U.A.
Evidence that acrosin activity is important for the development of fusibility of mammalian spermatozoa with the oolemma: inhibitor studies using the golden hamster
Zygote
1
79-91
1993
Mesocricetus auratus
brenda
Adekunle, A.O.; Storey, B.T.; Teuscher, C.
Guinea pig testicular proacrosin-acrosin system: further characterization of the active enzyme
Biol. Reprod.
40
127-134
1989
Cavia porcellus
brenda
Palencia, D.D.; Garner, D.L.; Hudig, D.; Holcombe, D.W.; Burner, C.A.; Redelman, D.; Fernandez, G.C.J.; Abuelyaman, A.S.; Kam, C.M.; Powers, J.C.
Determination of activable proacrosin/acrosin in bovine sperm using an irreversible isocoumarin serine protease inhibitor
Biol. Reprod.
55
536-542
1996
Bos taurus
brenda
Hoshi, K.; Sugano, T.; Yoshimatsu, N.; Yanagida, K.
Correlation of semen characteristics with acrosin, hyaluronidase, tubulin, dynein, and actin of spermatozoa
Arch. Androl.
35
165-172
1995
Homo sapiens
brenda
Suter, L.; Habenicht, U.F.
Characterization of mouse epididymal acrosin: comparative studies with acrosin from boar and human ejaculated spermatozoa
Int. J. Androl.
21
95-104
1998
Homo sapiens, Mus musculus, Sus scrofa
brenda
Zheng, X.L.; Geiger, M.; Ecke, S.; Resch, I.; Eberspaechler, U.; Donner, P.; Schleuning, W.D.; Binder, B.R.
Serine protease inhibitors (serpins) in human seminal plasma: concentrations and inhibition of acrosin
Fibrinolysis
8
364-371
1994
Sus scrofa
-
brenda
NagDas, S.K.
Bovine epididymal sperm proacrosin-acrosin system: quantification and partial characterization
Andrologia
24
171-178
1992
Bos taurus
brenda
Richardson, M.E.; Korn, N.; Bodine, A.B.; Thurston, R.J.
Research note: kinetic and inhibition studies with turkey acrosin
Poult. Sci.
71
1789-1793
1992
Meleagris gallopavo
brenda
Froman, D.P.
Chicken acrosin: extraction and purification
Poult. Sci.
69
812-817
1990
Gallus gallus
brenda
Smith, R.; Jenkins, A.; Lourbakos, A.; Thompson, P.; Ramakrishnan, V.; Tomlinson, J.; Deshpande, U.; Johnson, D.A.; Jones, R.; Mackie, E.J.; Pike, R.N.
Evidence for the activation of PAR-2 by the sperm protease, acrosin: expression of the receptor on oocytes
FEBS Lett.
484
285-290
2000
Sus scrofa
brenda
Hermans, J.M.; Haines, D.S.; James, P.S.; Jones, R.
Kinetics of inhibition of sperm beta-acrosin activity by suramin
FEBS Lett.
544
119-122
2003
Ovis aries, Sus scrofa
brenda
Tranter, R.; Read, J.A.; Jones, R.; Brady, R.L.
Effector sites in the three-dimensional structure of mammalian sperm beta-acrosin
Structure Fold. Des.
8
1179-1188
2000
Sus scrofa (P08001), Ovis aries (Q9GL10)
brenda
Rosatti, M.I.; Beconi, M.T.; Cordoba, M.
Proacrosin-acrosin activity in capacitated and acrosome reacted sperm from cryopreserved bovine semen
Biocell
28
311-316
2004
Bos taurus
brenda
Langlois, M.R.; Oorlynck, L.; Vandekerckhove, F.; Criel, A.; Bernard, D.; Blaton, V.
Discrepancy between sperm acrosin activity and sperm morphology: significance for fertilization in vitro
Clin. Chim. Acta
351
121-129
2005
Homo sapiens
brenda
Chaudhury, K.; Das, T.; Chakravarty, B.; Bhattacharyya, A.K.
Acrosin activity as a potential marker for sperm membrane characteristics in unexplained male infertility
Fertil. Steril.
83
104-109
2005
Homo sapiens
brenda
Furlong, L.I.; Harris, J.D.; Vazquez-Levin, M.H.
Binding of recombinant human proacrosin/acrosin to zona pellucida (ZP) glycoproteins. I. Studies with recombinant human ZPA, ZPB, and ZPC
Fertil. Steril.
83
1780-1790
2005
Homo sapiens
brenda
Furlong, L.I.; Veaute, C.; Vazquez-Levin, M.H.
Binding of recombinant human proacrosin/acrosin to zona pellucida glycoproteins. II. Participation of mannose residues in the interaction
Fertil. Steril.
83
1791-1796
2005
Homo sapiens
brenda
Gupta, G.; Jain, R.K.; Maikhuri, J.P.; Shukla, P.K.; Kumar, M.; Roy, A.K.; Patra, A.; Singh, V.; Batra, S.
Discovery of substituted isoxazolecarbaldehydes as potent spermicides, acrosin inhibitors and mild anti-fungal agents
Hum. Reprod.
20
2301-2308
2005
Homo sapiens
brenda
Gaboriau, D.; Howes, E.A.; Clark, J.; Jones, R.
Binding of sperm proacrosin/beta-acrosin to zona pellucida glycoproteins is sulfate and stereodependent. Synthesis of a novel fertilization inhibitor
Dev. Biol.
306
646-657
2007
Sus scrofa
brenda
Emokpae, M.A.; Uadia, P.O.
Acrosin activity in spermatozoa of infertile Nigerian males
Indian J. Clin. Biochem.
21
199-201
2006
Homo sapiens
brenda
Raterman, D.; Springer, M.S.
The molecular evolution of acrosin in placental mammals
Mol. Reprod. Dev.
75
1196-1207
2008
Canis lupus familiaris, Macaca mulatta, Amblysomus hottentotus (B0LM06), Echinops telfairi (B0LM07), Procavia capensis (B0LM08), Elephantulus edwardii (B0LM09), Galegeeska rufescens (B0LM10), Macroscelides proboscideus (B0LM11), Loxodonta africana (B0LM12), Dugong dugon (B0LM13), Trichechus manatus (B0LM14), Orycteropus afer (B0LM15), Bradypus tridactylus (B0LM16), Euphractus sexcinctus (B0LM17), Felis catus (B0LM18), Puma concolor (B0LM19), Tursiops truncatus (B0LM20), Lama glama (B0LM21), Tragelaphus angasii (B0LM22), Tadarida brasiliensis (B0LM23), Sorex cinereus (B0LM24), Talpa europaea (B0LM25), Diceros bicornis (B0LM26), Equus caballus (B0LM27), Tapirus pinchaque (B0LM28), Manis sp. DMR-2008 (B0LM29), Cynocephalus volans (B0LM30), Tupaia glis (B0LM31), Ochotona princeps (B0LM32), Sylvilagus floridanus (B0LM33), Pan troglodytes (B0LM34), Hystrix brachyura (B0LM35), Erethizon dorsatum (B0LM36), Rattus fuscipes (B0LM37), Otospermophilus beecheyi (B0LM38), Sus scrofa (P08001), Homo sapiens (P10323), Homo sapiens, Rattus norvegicus (P29293), Oryctolagus cuniculus (P48038), Bos taurus (P79343), Mus musculus (Q3ZB05), Cavia porcellus (Q60491), Ovis aries (Q9GL10)
brenda
Veaute, C.; Furlong, L.I.; Bronson, R.; Harris, J.D.; Vazquez-Levin, M.H.
Acrosin antibodies and infertility. I. Detection of antibodies towards proacrosin/acrosin in women consulting for infertility and evaluation of their effects upon the sperm protease activities
Fertil. Steril.
91
1245-1255
2009
Homo sapiens
brenda
Veaute, C.; Furlong, L.I.; Cameo, M.; Harris, J.D.; Vazquez-Levin, M.H.
Antiacrosin antibodies and infertility. II. Gene immunization with human proacrosin to assess the effect of immunity toward proacrosin/acrosin upon protein activities and animal fertility
Fertil. Steril.
91
1256-1268
2009
Homo sapiens
brenda
Aquila, S.; Guido, C.; Santoro, A.; Perrotta, I.; Laezza, C.; Bifulco, M.; Sebastiano, A.
Human sperm anatomy: ultrastructural localization of the cannabinoid1 receptor and a potential role of anandamide in sperm survival and acrosome reaction
Anat. Rec. (Hoboken)
293
298-309
2010
Homo sapiens
brenda
Psenicka, M.; Vancova, M.; Koubek, P.; Tesitel, J.; Linhart, O.
Fine structure and morphology of sterlet (Acipenser ruthenus L. 1758) spermatozoa and acrosin localization
Anim. Reprod. Sci.
111
3-16
2009
Acipenser ruthenus, Acipenser ruthenus 1758
brenda
Davidova, N.; Jonakova, V.; Manaskova-Postlerova, P.
Expression and localization of acrosin inhibitor in boar reproductive tract
Cell Tissue Res.
338
303-311
2009
Sus scrofa
brenda
Yin, L.; Hang, T.; Zhang, Z.
Determination of 4-carbomethoxyphenyl 4-guanidinobenzoate mesylate by HPLC and identification of its related substances by LC-MS-MS
J. Chromatogr. Sci.
47
872-876
2009
Homo sapiens
brenda
De los Reyes, M.; Medina, G.; Palomino, J.
Western blot analysis of proacrosin/acrosin in frozen dog sperm during in vitro capacitation
Reprod. Domest. Anim.
44 Suppl 2
350-353
2009
Canis lupus familiaris
brenda
Qi, J.; Zhu, J.; Liu, X.; Ding, L.; Zheng, C.; Han, G.; Lv, J.; Zhou, Y.
Synthesis and acrosin inhibitory activities of substituted ethyl 5-(4-aminophenyl)-1H-pyrazole-3-carboxylate derivatives
Bioorg. Med. Chem. Lett.
21
5822-5825
2011
Homo sapiens
brenda
Ding, L.; Zhu, J.; Zheng, C.; Sheng, C.; Qi, J.; Liu, X.; Han, G.; Zhao, J.; Lv, J.; Zhou, Y.
Synthesis and acrosin inhibitory activity of substituted 4-amino-N-(diaminomethylene) benzenesulfonamide derivatives
Bioorg. Med. Chem. Lett.
21
6674-6677
2011
Homo sapiens
brenda
Jiang, J.; Liu, X.; Zhen, C.; Zhou, Y.; Zhu, J.; Lv, J.; Sheng, C.
Acrosin structure-based design, synthesis and biological activities of 7-azaindol derivatives as new acrosin inhibitors
Chin. Chem. Lett.
22
272-275
2011
Homo sapiens
-
brenda
Slowinska, M.; Olczak, M.; Liszewska, E.; Watorek, W.; Ciereszko, A.
Isolation, characterization and cDNA sequencing of acrosin from turkey spermatozoa
Comp. Biochem. Physiol. B
157
127-136
2010
Meleagris gallopavo (Q2UVH8), Meleagris gallopavo
brenda
Liu, X.; Dong, G.; Zhang, J.; Qi, J.; Zheng, C.; Zhou, Y.; Zhu, J.; Sheng, C.; Lue, J.
Discovery of novel human acrosin inhibitors by virtual screening
J. Comput. Aided Mol. Des.
25
977-985
2011
Homo sapiens
brenda
Sasanami, T.; Yoshizaki, N.; Dohra, H.; Kubo, H.
Sperm acrosin is responsible for the sperm binding to the egg envelope during fertilization in Japanese quail (Coturnix japonica)
Reproduction
142
267-276
2011
Coturnix japonica
brenda
Liu, X.; Chen, Q.; Zhu, J.; Fan, Y.; Ding, L.; Zhao, J.; Han, G.; Tian, W.; Qi, J.; Zhou, Y.; Lv, J.
Synthesis and acrosin inhibitory activity of methyl 5-substituted-1H-benzo[d]imidazol-2-yl carbamate derivatives
Bioorg. Med. Chem. Lett.
22
3554-3559
2012
Homo sapiens
brenda
Zhao, J.; Tian, W.; Qi, J.; Lv, D.; Liu, Y.; Jiang, Y.; Dong, G.; Chen, Q.; Zhou, Y.; Zhu, J.; Wang, H.; Sheng, C.; Lv, J.
Design and synthesis of phenylisoxazole derivatives as novel human acrosin inhibitors
Bioorg. Med. Chem. Lett.
24
2802-2806
2014
Homo sapiens
brenda
Ferrer, M.; Rodriguez, H.; Zara, L.; Yu, Y.; Xu, W.; Oko, R.
MMP2 and acrosin are major proteinases associated with the inner acrosomal membrane and may cooperate in sperm penetration of the zona pellucida during fertilization
Cell Tissue Res.
349
881-895
2012
Bos taurus
brenda
Chen, Q.; Tian, W.; Han, G.; Qi, J.; Zheng, C.; Zhou, Y.; Ding, L.; Zhao, J.; Zhu, J.; Lv, J.; Sheng, C.
Design and synthesis of novel benzoheterocyclic derivatives as human acrosin inhibitors by scaffold hopping
Eur. J. Med. Chem.
59
176-182
2013
Homo sapiens
brenda
Slowinska, M.; Ciereszko, A.
Identification of the second form of acrosin in Turkey spermatozoa
Reprod. Domest. Anim.
47
849-855
2012
Meleagris gallopavo
brenda
Perez Aguirreburualde, M.S.; Fernandez, S.; Cordoba, M.
Acrosin activity regulation by protein kinase C and tyrosine kinase in bovine sperm acrosome exocytosis induced by lysophosphatidylcholine
Reprod. Domest. Anim.
47
915-920
2012
Bos taurus
brenda
Slowinska, M.; Liszewska, E.; Dietrich, G.J.; Ciereszko, A.
Characterization of proacrosin/acrosin system after liquid storage and cryopreservation of turkey semen (Meleagris gallopavo)
Theriogenology
78
1065-1077
2012
Meleagris gallopavo
brenda
Zhang, G.; Yang, W.; Zou, P.; Jiang, F.; Zeng, Y.; Chen, Q.; Sun, L.; Yang, H.; Zhou, N.; Wang, X.; Liu, J.; Cao, J.; Zhou, Z.; Ao, L.
Mitochondrial functionality modifies human sperm acrosin activity, acrosome reaction capability and chromatin integrity
Hum. Reprod.
34
3-11
2019
Homo sapiens
brenda
Xu, F.; Zhu, H.; Zhu, W.; Fan, L.
Human sperm acrosomal status, acrosomal responsiveness, and acrosin are predictive of the outcomes of in vitro fertilization A prospective cohort study
Reprod. Biol.
18
344-354
2018
Homo sapiens
brenda
Pinart, E.; Yeste, M.; Bonet, S.
Acrosin activity is a good predictor of boar sperm freezability
Theriogenology
83
1525-1533
2015
Sus scrofa
brenda
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