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Enzyme Nomenclature
Information on EC 3.4.21.10 - acrosin
for references in articles please use BRENDA:EC3.4.21.10
Word Map on EC 3.4.21.10
- 3.4.21.10
- spermatozoa
- boar
- semen
- trypsin
-
ejaculate
-
seminal
- pellucida
- oocyte
-
infertile
-
capacitation
-
trypsin-like
- epididymal
-
contraceptive
-
bull
- gamete
-
zymogen
-
spermatogenesis
- hyaluronidase
- benzamidine
-
kallikreins
-
autoactivation
- cauda
-
insemination
-
acrosome-reacted
-
spermatid
-
antifertility
-
acrosome-intact
- medicine
-
fucoidan
- p-aminobenzamidine
-
sperm-zona
-
gelatinolytic
-
andrology
-
sperm-associated
-
zona-free
- tlck
-
sperm-oocyte
-
nonoxynol-9
-
amidolytic
-
sperm-egg
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Specify your search results
The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.4.21.10
-
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RECOMMENDED NAME
GeneOntology No.
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
36461, 36462, 36468, 36474, 36479, 36483, 36484, 668680, 668887, 692404, 692405, 707132, 709265, 717353, 717359, 717498, 717912, 731432, 731451, 731747
-
-
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
-
-
patients with unexplained infertility and infertile males with low motility of semen
-
-
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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
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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-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
-
-
-
-
?
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
?
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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
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
B0LM06
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
P79343
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
B0LM16
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
Q60491
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
B0LM30
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
B0LM26
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
B0LM13
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
B0LM07
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
B0LM09
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
B0LM10
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
B0LM27
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
B0LM36
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
B0LM17
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
B0LM18
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
P10323
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
B0LM35
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
B0LM21
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
B0LM12
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
B0LM11
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
B0LM29
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
Q3ZB05
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
B0LM32
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
B0LM15
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
P48038
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
B0LM38
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
Q9GL10
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
B0LM34
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
B0LM08
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
B0LM19
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
B0LM37
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
P29293
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
B0LM24
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
P08001
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
B0LM33
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
B0LM23
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
B0LM25
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
B0LM28
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
B0LM22
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
B0LM14
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
B0LM31
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
B0LM20
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
additional information
?
-
B0LM06
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
?
-
P79343
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM16
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
?
-
Q60491
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM30
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM26
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM13
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM07
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM09
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM10
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM27
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM36
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM17
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM18
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
?
-
P10323
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM35
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM21
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM12
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
?
-
B0LM11
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM29
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
?
-
Q3ZB05
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM32
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM15
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
?
-
P48038
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM38
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
?
-
Q9GL10
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM34
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM08
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM19
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM37
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
P29293
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM24
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
?
-
P08001
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM33
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM23
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM25
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM28
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM22
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM14
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM31
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
additional information
?
-
B0LM20
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.
INHIBITORS
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
-
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
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
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
-
the protein is distributed on the surface and in the acrosomal matrix of the sperm head
-
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
-
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
-
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
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
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
-
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
-
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
-
acrosin is expressed in the testis, where it is stored in the acrosomal cap of sperm in its inactive form, proacrosin
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE