Information on EC 3.4.21.10 - acrosin

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The expected taxonomic range for this enzyme is: Euteleostomi

EC NUMBER
COMMENTARY
3.4.21.10
-
RECOMMENDED NAME
GeneOntology No.
acrosin
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential cleavage: Arg-/-, Lys-/-
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53 kDa fucose-binding protein
-
-
-
-
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
-
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
-
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin
trypsin-like serine protease of the S1 family
acrosin amidase
-
-
-
-
acrosin amidase
-
-
acrosin I
-
isoform
acrosin II
-
isoform
acrosomal protease
-
-
-
-
acrosomal proteinase
-
-
-
-
acrozonase
-
-
-
-
alpha-acrosin
-
-
-
-
beta-acrosin
-
-
-
-
beta-acrosin
-
residues 1-322, activated form of proacrosin (residues 1-399)
proteinase, acrosomal
-
-
-
-
psi-acrosin
-
-
-
-
sperm acrosin
-
-
CAS REGISTRY NUMBER
COMMENTARY
9068-57-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 1758
-
-
Manually annotated by BRENDA team
Acipenser ruthenus 1758
strain 1758
-
-
Manually annotated by BRENDA team
Hottentot golden mole
SwissProt
Manually annotated by BRENDA team
bovine proacrosine
SwissProt
Manually annotated by BRENDA team
fragment; pale-throated three-toed sloth
SwissProt
Manually annotated by BRENDA team
goat
-
-
Manually annotated by BRENDA team
preproacrosin, precursor, fragment; guinea pig
SwissProt
Manually annotated by BRENDA team
japanese quail
-
-
Manually annotated by BRENDA team
fragment; Philippine flying lemur
SwissProt
Manually annotated by BRENDA team
black rhinoceros
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
lesser hedgehog tenrec
SwissProt
Manually annotated by BRENDA team
fragement; Cape long-eared elephant shrew
SwissProt
Manually annotated by BRENDA team
fragment; East African long-eared elephant shrew
SwissProt
Manually annotated by BRENDA team
fragment; horse
SwissProt
Manually annotated by BRENDA team
fragment; North American porcupine
SwissProt
Manually annotated by BRENDA team
fragment; six-banded armadillo
SwissProt
Manually annotated by BRENDA team
fragment; cat
SwissProt
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
infertile couples
-
-
Manually annotated by BRENDA team
patients with unexplained infertility and infertile males with low motility of semen
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
recombinant protein
-
-
Manually annotated by BRENDA team
fragment; Malayan porcupine
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment; African elephant
SwissProt
Manually annotated by BRENDA team
fragment; short-eared elephant shrew
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
fragment; Southern American pika
SwissProt
Manually annotated by BRENDA team
fragment; Aardvark
SwissProt
Manually annotated by BRENDA team
3 forms with different molecular weight
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
fragment; Beechey ground squirrel
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
beta-acrosin, psi-acrosin
-
-
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
fragment; chimpanzee
SwissProt
Manually annotated by BRENDA team
fragment; rock dassie
SwissProt
Manually annotated by BRENDA team
fragment; mountain lion
SwissProt
Manually annotated by BRENDA team
fragment; bush rat
SwissProt
Manually annotated by BRENDA team
precursor
SwissProt
Manually annotated by BRENDA team
fragment; masked shrew
SwissProt
Manually annotated by BRENDA team
alpha-acrosin, beta-acrosin; male
-
-
Manually annotated by BRENDA team
proacrosin nucleotides 22-849
UniProt
Manually annotated by BRENDA team
fragment; cottontail rabbit
SwissProt
Manually annotated by BRENDA team
fragment; Brazilian free-tailed bat
SwissProt
Manually annotated by BRENDA team
fragment; European mole
SwissProt
Manually annotated by BRENDA team
fragment; mountain tapir
SwissProt
Manually annotated by BRENDA team
fragment; nyala
SwissProt
Manually annotated by BRENDA team
fragment; Caribbean manatee, West Indian manatee
SwissProt
Manually annotated by BRENDA team
fragment; tree shrew
SwissProt
Manually annotated by BRENDA team
fragment; Atlantic bottle-nosed dolphin
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
acrosin is responsible for the serine protease activity associated with the inner acrosomal membrane
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
aminobenzoyl-Ser-Lys-Gly-Arg-Ser-Leu-Ile-Gly-Lys(dinitrophenyl)-Asp + H2O
?
show the reaction diagram
-
-
-
-
?
collagen I + H2O
?
show the reaction diagram
-
heat denatured
-
-
?
Collagen IV + H2O
?
show the reaction diagram
-
-
-
-
?
D-valyl-L-leucyl-L-arginine p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-alpha-benzoyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-benzoyl-DL-arginine-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-DL-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-DL-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-DL-arginine-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-DL-lysine p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide hydrochloride + H2O
?
show the reaction diagram
-
-
-
-
-
Nalpha-benzoyl-L-arginine beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester hydrochloride + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-tosyl-L-arginine methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-tosyl-L-arginine methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
proacrosin + H2O
acrosin + ?
show the reaction diagram
-
-
-
?
proacrosin + H2O
acrosin + ?
show the reaction diagram
-
-
-
?
proacrosin + H2O
acrosin + ?
show the reaction diagram
-
-
-
?
proacrosin + H2O
acrosin + ?
show the reaction diagram
-
-
-
?
proacrosin + H2O
acrosin + peptide
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
?
show the reaction diagram
-
the enzyme may play additional role(s) in the fertilization process via the activation of PAR-2 on oocytes
-
-
?
toluene-p-sufonyl-L-arginine methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
toluene-p-sulfonyl-L-arginine methyl ester hydrochloride + H2O
?
show the reaction diagram
-
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
-
?
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
?
-
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
possibly important for fertilization process, involved in the acrosome reaction, binding of spermatozoa to and penetration through the zona pellucida
-
-
-
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
-
-
-
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
?
-
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
?
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
proacrosin + H2O
acrosin + ?
show the reaction diagram
-
-
-
?
proacrosin + H2O
acrosin + ?
show the reaction diagram
-
-
-
?
proacrosin + H2O
acrosin + ?
show the reaction diagram
-
-
-
?
proacrosin + H2O
acrosin + ?
show the reaction diagram
-
-
-
?
proacrosin + H2O
acrosin + peptide
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
B0LM20
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
P48038
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
?
show the reaction diagram
-
the enzyme may play additional role(s) in the fertilization process via the activation of PAR-2 on oocytes
-
-
?
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
?
-
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
P29293
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM34
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
Q9GL10
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM07
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM06
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM08
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM09
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM10
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM11
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM12
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM13
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM15
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM14
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM16
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM17
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
Q3ZB05
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM18
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM19
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM20
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
P08001
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM21
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM22
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM23
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM24
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM25
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM26
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM27
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM28
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM29
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM30
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
P79343
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM31
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM32
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM33
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM38
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM35
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM36
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
B0LM37
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
Q60491
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
P10323
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
P48038
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
possibly important for fertilization process, involved in the acrosome reaction, binding of spermatozoa to and penetration through the zona pellucida
-
-
-
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
?
-
P29293
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
?
-
Q9GL10
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
?
-
B0LM06
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
?
-
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
?
-
B0LM11
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
?
-
B0LM13
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
?
-
B0LM14
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
?
-
B0LM17
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
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
?
-
B0LM18
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
?
-
B0LM20
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
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
?
-
B0LM21
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
?
-
B0LM23
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
?
-
B0LM25
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
?
-
B0LM27
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
?
-
B0LM29
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
?
-
P79343
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
?
-
B0LM32
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
?
-
B0LM38
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
?
-
B0LM36
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
?
-
Q60491
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
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
?
-
P48038
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
activates
Ca2+
-
activates
Ca2+
-
activates
Ca2+
-
activates
Mg2+
-
activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(2, 4-dichlorobenzoyl)-N-methyl-1H-indazole-3-carboxamide
-
-
-
2,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
2,6-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
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-(3-(3-hydroxyethyl)ureido)-N-(2-methoxybenzyl)-1H-benzo[d]imidazole-5-sulfonamide
-
-
-
2-(4-chlorophenoxy)-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]acetamide
-
-
2-bromo-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
2-chloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
2-mercaptoethanol
-
-
3,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
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)-1,2-oxazole-5-carbaldehyde
-
-
3-(4-nitrophenyl)isoxazole-5-carbaldehyde
-
50% inhibition at 0.42 mM, weak antifungal activity against Candida albicans
3-chloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
3-methylbutyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
3-[4-([[4-(aminomethyl)cyclohexyl]carbonyl]oxy)phenyl]propanoic acid
-
-
4-(4'-aminophenoxypropoxy)benzamidine
-
-
-
4-(4'-nitrophenyl)guanidinobenzoate
-
-
-
4-(acetylamino)phenyl 4-carbamimidamidobenzoate
-
-
4-(chloromethyl)-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
4-([4-[3-(ethoxycarbonyl)-1H-pyrazol-5-yl]phenyl]amino)-4-oxobutanoic acid
-
-
4-aminobenzamidine
-
-
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
4-nitrophenyl-4'-guanidine benzoate
-
-
-
4-[(2-methylbenzyl)(methylsulfonyl)amino]-N-(pyridin-4-ylmethyl)benzamide
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5-(2,4-dichlorophenyl)-1,2-oxazole-3-carbaldehyde
-
-
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 hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(2,3-dimethylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(2,4-dimethoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(2,5-dimethoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(2,6-dimethylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(2-methoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(2-methylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(3,5-dimethylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(3-chlorophenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(3-methoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(3-methylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(4-chlorophenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(4-cyanophenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(4-ethoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(4-fluorophenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(4-methylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(4-methylpyridin-2-yl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(naphthalen-1-yl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-(propan-2-yl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
5-(4-carbamimidamidophenyl)-N-phenyl-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
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-([4-[3-(ethoxycarbonyl)-1H-pyrazol-5-yl]phenyl]amino)-5-oxopentanoic acid
-
-
5-Aminovaleric acid
-
-
5-phenylisoxazole-3-carbaldehyde
-
50% inhibition at 2.4 mM, weak antifungal activity against Candida albicans
6-Aminocaproic acid
-
-
7-amino-1-chloro-3-L-tosylamidoheptan-2-one
-
weak
Alpha1-antitrypsin
-
-
-
antipain
-
-
antithrombin
-
-
-
antithrombin
-
III
-
Aprotinin
-
-
Aprotinin
-
-
Aprotinin
-
-
benzamidine
-
-
benzamidine
-
-
benzamidine
-
-
benzamidine
-
-
Benzamidine hydrochloride
-
50% inhibition at 2.2 mM, weak antifungal activity against Candida albicans
butan-1-ol
-
-
butyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
Ca2+
-
-
D-arabinose
-
-
D-fructose
-
-
dacarbazine
-
BIC
diaminomethylene-benzenesulfonamide
-
-
-
diisopropylfluorophosphate
-
weak
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
dithiothreitol
-
-
ethyl 1-(2, 4-dichlorobenzoyl)-1H-indazole-3-carboxylate
-
-
-
ethyl 1-(phenylcarbonyl)-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-(thiophen-2-ylcarbonyl)-1H-pyrrolo[2,3-b]pyridine-3-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-[(2-chlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-methoxyphenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-methylphenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(3,4-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(3-fluorophenyl)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-(acetylamino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-(benzoylamino)phenyl]-1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-(butanoylamino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-(pentanoylamino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-(propanoylamino)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
-
-
ethyl 5-[4-[(2-chlorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-[(3,4-dichlorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-[(3-chloropropanoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(4-benzylbenzoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(4-chlorobenzoyl)amino]phenyl]1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-[(4-fluorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-[(phenylcarbonyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(trifluoroacetyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
guanidinobenzoate
-
KF950
Hg2+
-
-
human protein C inhibitor
-
-
-
iodoacetate
-
-
iodoacetate
-
-
Kazal seminal plasma inhibitor
-
-
L-1-chloro-3-[4-tosylamido]-7-amino-2-heptanone
-
-
L-arginine
-
esterolytic activity
L-histidine
-
weak
L-homoarginine
-
-
Leupeptin
-
-
Leupeptin
-
-
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
-
-
methyl [6-(butylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-(hexylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-(phenylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-(propan-2-ylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2,5-dimethylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3,4-dimethoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-bromophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[benzyl(methyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
N,N-bis(2-hydroxyethyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
-
-
-
N,N-dibenzyl-2-[4-(propan-2-ylsulfamoyl)phenoxy]acetamide
-
-
N-(2-bromophenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
-
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-(2-hydroxyethyl)-5-(4-methoxyphenyl)-N-methyl-1H-pyrazole-3-carboxamide
-
-
-
N-(2-hydroxypropyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
-
-
-
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-(3-hydroxypropyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
-
-
-
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-(5-bromobenzo[d]thiazol-2-yl)-2-(4-pentylpiperazin-1-yl)acetamide
-
-
-
N-(5-bromobenzo[d]thiazol-2-yl)-2-(diisopentylamino)acetamide
-
-
-
N-(5-bromobenzo[d]thiazol-2-yl)-2-(dipentylamino)acetamide
-
-
-
N-(6-bromobenzo[d]thiazol-2-yl)-2-(dibutylamino) acetamide
-
-
-
N-alpha-tosyl-L-lysyl-chloromethyl-ketone
-
-
-
N-alpha-tosyl-L-lysyl-chloromethylketone
-
-
N-benzyl-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
-
N-cyclohexyl-2-[(4,6-diphenylpyrimidin-2-yl)sulfanyl]acetamide
-
-
N-hexyl-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
-
N-tosyl-L-lysine chloromethylketone
-
-
N-[4-(dipropylsulfamoyl)phenyl]-3,4-diethoxybenzamide
-
-
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-[(4-fluorophenyl)sulfamoyl]phenyl]-3,4,5-trimethoxybenzamide
-
-
N-[4-[(4-methoxyphenyl)sulfamoyl]phenyl]-2-(naphthalen-1-yloxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2,4,6-trimethylbenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2,6-difluorobenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylphenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylpiperidin-1-yl)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(3-methylphenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methoxyphenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylphenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylpiperidin-1-yl)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-nitrophenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(piperidin-1-yl)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-phenoxyacetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3,5-dinitrobenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3-(trifluoromethyl)benzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethoxybenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethylbenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-fluorobenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methoxybenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methylbenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]butanamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]pentanamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]propanamide
-
-
Nalpha-benzoyl-DL-arginine p-nitroanilide
-
-
Nalpha-tosyl-L-lysine chloromethyl ketone
-
-
Nalpha-tosyl-L-lysine chloromethyl ketone
-
-
Nalpha-tosyl-L-lysine chloromethyl ketone
-
-
Nalpha-tosyl-L-lysine chloromethyl ketone
-
-
Nalpha-tosyl-L-phenylalanyl-chloromethane
-
-
nexin 1
-
-
-
NF064
-
-
NSC651015
-
-
NSC651016
-
-
ovomucoid
-
chicken
-
ovomucoid
-
-
-
ovomucoid
-
-
-
p-aminobenzamidine
-
-
p-aminobenzamidine
-
-
p-hydroxymercuribenzoate
-
-
phenylmethylsulfonyl fluoride
-
-
phenylpyrazole
-
-
-
plasminogen activator inhibitor-1
-
-
plasminogen activator inhibitor-2
-
-
-
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
-
-
Proteinase inhibitors
-
-
-
quinazolinone
-
-
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
-
-
Trypsin inhibitor
-
soybean
-
Trypsin inhibitor
-
bovine pancreatic; lima-bean; soybean
-
Trypsin inhibitor
-
soybean
-
Trypsin inhibitor
-
lima-bean
-
Trypsin inhibitor
-
soybean
-
Trypsin inhibitor
-
soybean
-
Trypsin inhibitor II
-
-
-
Trypsin-plasmin inhibitor
-
bdellin B-3
-
methyl [6-[bis(3-methylbutyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
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
-
mechanism of inhibition
-
additional information
-
no inhibition with quercetin-3beta-D-glucoside or quercetin-3beta-D-glucoside sulfate
-
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
progesterone
-
up to 2fold activation
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
-
additional information
-
not activating: heparin, quercitin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.65
Nalpha-benzoyl-DL-lysine p-nitroanilide
-
-
0.44
Nalpha-benzoyl-L-arginine ethyl ester
-
-
0.28
Nalpha-benzoyl-L-arginine ethyl ester hydrochloride
-
-
1.1
Nalpha-benzoyl-L-arginine p-nitroanilide
-
-
2.7
Nalpha-benzyol-L-arginine beta-naphthylamide
-
-
-
0.77
Nalpha-tosyl-L-arginine methyl ester
-
-
0.021
toluene-p-sulfonyl-L-arginine methyl ester
-
-
0.022
aminobenzoyl-Ser-Lys-Gly-Arg-Ser-Leu-Ile-Gly-Lys(dinitrophenyl)-Asp
-
pH 7.4, 37C
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
115 - 162
Nalpha-benzoyl-L-Arg ethyl ester
Ovis aries
-
-
49
toluene-p-sulfonyl-L-arginine methyl ester hydrochloride
Ovis aries
-
-
-
320
aminobenzoyl-Ser-Lys-Gly-Arg-Ser-Leu-Ile-Gly-Lys(dinitrophenyl)-Asp
Sus scrofa
-
pH 7.4, 37C
additional information
additional information
Homo sapiens
-
-
-
additional information
additional information
Ovis aries
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.28
3-(4-nitrophenyl)isoxazole-5-carbaldehyde
-
pH 8.0, 37C
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
-
7.32
2-(3-(3-hydroxyethyl)ureido)-N-(2-methoxybenzyl)-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
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 37C
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 37C
0.008
4-(acetylamino)phenyl 4-carbamimidamidobenzoate
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
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 37C
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 37C
0.39
5-(2,4-dichlorophenyl)-1,2-oxazole-3-carbaldehyde
Homo sapiens
-
pH 7.8, 37.8C
1.7
5-(2,4-dichlorophenyl)-1,2-oxazole-3-carbaldehyde
Homo sapiens
-
pH 8.0, 22C
0.1
5-(4-carbamimidamidophenyl)-N-(1-hydroxypropan-2-yl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0115
5-(4-carbamimidamidophenyl)-N-(2,3-dimethylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0014
5-(4-carbamimidamidophenyl)-N-(2,4-dimethoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0023
5-(4-carbamimidamidophenyl)-N-(2,5-dimethoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0057
5-(4-carbamimidamidophenyl)-N-(2,6-dimethylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0084
5-(4-carbamimidamidophenyl)-N-(2-methoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0144
5-(4-carbamimidamidophenyl)-N-(2-methylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0121
5-(4-carbamimidamidophenyl)-N-(3,5-dimethylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0254
5-(4-carbamimidamidophenyl)-N-(3-chlorophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0066
5-(4-carbamimidamidophenyl)-N-(3-methoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0094
5-(4-carbamimidamidophenyl)-N-(3-methylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0268
5-(4-carbamimidamidophenyl)-N-(4-chlorophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0239
5-(4-carbamimidamidophenyl)-N-(4-cyanophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0064
5-(4-carbamimidamidophenyl)-N-(4-ethoxyphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0205
5-(4-carbamimidamidophenyl)-N-(4-fluorophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0101
5-(4-carbamimidamidophenyl)-N-(4-methylphenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0214
5-(4-carbamimidamidophenyl)-N-(4-methylpyridin-2-yl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0299
5-(4-carbamimidamidophenyl)-N-(naphthalen-1-yl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.1
5-(4-carbamimidamidophenyl)-N-(propan-2-yl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0246
5-(4-carbamimidamidophenyl)-N-phenyl-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
0.0203
5-(4-carbamimidamidophenyl)-N-[4-(trifluoromethyl)phenyl]-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
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, 37.8C
-
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, 37.8C
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, 37.8C
0.24
ethyl 5-[4-[(3,4-dichlorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8C
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, 37.8C
0.14
ethyl 5-[4-[(4-fluorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8C
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
0.000027
KF950
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, 22C
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 37C
1.77
methyl [6-(butylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
1.8
methyl [6-(hexylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
1.03
methyl [6-(phenylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
0.47
methyl [6-(propan-2-ylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
1.27
methyl [6-[(2,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
1.55
methyl [6-[(2,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
8.86
methyl [6-[(2,5-dimethylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
5.75
methyl [6-[(2-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
0.31
methyl [6-[(2-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
8.42
methyl [6-[(2-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
4.02
methyl [6-[(3,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
1.59
methyl [6-[(3,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
11.5
methyl [6-[(3,4-dimethoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
1.81
methyl [6-[(3-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
7.5
methyl [6-[(3-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
5.06
methyl [6-[(3-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
1.64
methyl [6-[(4-bromophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
7.52
methyl [6-[(4-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
2.4
methyl [6-[(4-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
3.29
methyl [6-[(4-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
3.18
methyl [6-[(4-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
1.25
methyl [6-[benzyl(methyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
0.063
methyl [6-[bis(3-methylbutyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22C
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 37C
0.0279
N-(2-bromophenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
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, 37.8C
-
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 37C
0.0078
N-(4-tert-butylphenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8C
-
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
-
0.1426
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 37C
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 37C
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 37C
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 37C
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 37C
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 37C
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 37C
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
0.012
NF064
Sus scrofa
-
23C
0.7
NSC651015
Sus scrofa
-
23C
0.7
NSC651016
Sus scrofa
-
23C
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
0.1
suramin
Sus scrofa
-
23C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12
-
-
37
-
-
49.23
-
-
92.9
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8.5
-
-
7.7
-
-
7.8
-
-
7.8
-
assay at
8
-
assay at
8.5
-
-
8.7
-
-
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 - 8.5
-
-
6.5 - 9.5
-
pH 6.5: about 50% of maximal activity, pH 9.5: about 25% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
-
assay at room temperature
37
-
assay at
53
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 65
-
about 15% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.4
isoelectric focusing
7.3
mature protein, calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Acipenser ruthenus 1758
-
-
-
Manually annotated by BRENDA team
-
from infertile men
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
acrosin is a major serine proteinase of mammalian sperm
Manually annotated by BRENDA team
-
the protein is distributed on the surface and in the acrosomal matrix of the sperm head
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
Acipenser ruthenus 1758
-
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
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Manually annotated by BRENDA team
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acrosin is expressed in the testis, where it is stored in the acrosomal cap of sperm in its inactive form, proacrosin
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Acipenser ruthenus 1758
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-
-
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Manually annotated by BRENDA team
Acipenser ruthenus 1758
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-
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Manually annotated by BRENDA team
additional information
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enzyme subcellular localization analysis, overview
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Manually annotated by BRENDA team
additional information
Acipenser ruthenus 1758
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enzyme subcellular localization analysis, overview
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-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
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gel filtration
36471
76000
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gel filtration
36462, 36468
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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x * 52000, x * 68000, x * 34000, SDS-PAGE, 3 forms with different molecular weight
?
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x * 34500, SDS-PAGE, beta-acrosin; x * 48000, SDS-PAGE, alpha-acrosin
?
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x * 39000, SDS-PAGE
?
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x * 49000, SDS-PAGE
?
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x * 38000, SDS-PAGE, beta-acrosin
?
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x * 38000, SDS-PAGE
?
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x * 30000, SDS-PAGE
?
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x * 27000, SDS-PAGE
?
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x * 58000-60000, SDS-PAGE, doublet
?
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x * 52000-54000, SDS-PAGE, doublet
?
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x * 55000-59000, SDS-PAGE, doublet
?
x * 30469, calculated from the deduced amino acid sequence
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x * 41722, calculated from the deduced amino acid sequence
?
x * 30066, calculated from the deduced amino acid sequence
?
x * 45773, calculated from the deduced amino acid sequence
?
x * 25649, calculated from the deduced amino acid sequence
?
x * 30707, calculated from the deduced amino acid sequence
?
x * 30515, calculated from the deduced amino acid sequence
?
x * 28794, calculated from the deduced amino acid sequence
?
x * 30616, calculated from the deduced amino acid sequence
?
x * 30809, calculated from the deduced amino acid sequence
?
x * 30679, calculated from the deduced amino acid sequence
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x * 30361, calculated from the deduced amino acid sequence
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x * 26300, calculated from the deduced amino acid sequence
?
x * 30583, calculated from the deduced amino acid sequence
?
x * 45847, calculated from the deduced amino acid sequence
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x * 30413, calculated from the deduced amino acid sequence
?
x * 30276, calculated from the deduced amino acid sequence
?
x * 30357, calculated from the deduced amino acid sequence
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x * 30628, calculated from the deduced amino acid sequence
?
x * 26896, calculated from the deduced amino acid sequence
?
x * 43016, calculated from the deduced amino acid sequence
?
x * 30310, calculated from the deduced amino acid sequence
?
x * 28582, calculated from the deduced amino acid sequence
?
x * 46422, calculated from the deduced amino acid sequence
?
x * 30604, calculated from the deduced amino acid sequence
?
x * 36119, calculated from the deduced amino acid sequence
?
x * 30233, calculated from the deduced amino acid sequence
?
x * 30583, calculated from the deduced amino acid sequence
?
x * 30455, calculated from the deduced amino acid sequence
?
x * 48623, calculated from the deduced amino acid sequence
?
x * 26746, calculated from the deduced amino acid sequence
?
x * 30534, calculated from the deduced amino acid sequence
?
x * 30138, calculated from the deduced amino acid sequence
?
x * 30202, calculated from the deduced amino acid sequence
?
x * 30788, calculated from the deduced amino acid sequence
?
x * 29689, calculated from the deduced amino acid sequence
?
x * 30556, calculated from the deduced amino acid sequence
?
x * 30452, calculated from the deduced amino acid sequence
?
x * 28577, calculated from the deduced amino acid sequence
?
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x * 40000, proacrosin, SDS-PAGE, x * 32000, alpha-acrosin, SDS-PAGE, x * 27000, beta-acrosin, SDS-PAGE
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x * 30000, active enzyme, SDS-PAGE; x * 30874, mass spectrometry; x * 360517, mature protein, calculated from amino acid sequence
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x * 45000, SDS-PAGE
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x * 35000, mature form, SDS-PAGE; x * 43000, immmature form, SDS-PAGE
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x * 30869, mass spectrometry; x * 41000, SDS-PAGE
?
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x * 30000, isoform acrosin I, SDS-PAGE; x * 41000, isoform acrosin II, SDS-PAGE
monomer
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1 * 76000, SDS-PAGE
monomer
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1 * 42000, SDS-PAGE
additional information
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interaction of protein with zona pellucida glycoproteins, highest binding activity toward glycoprotein ZPA
additional information
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proenzyme binds to bovine serum albumin-mannose, binding sites are stabilized by noncovalent bonds and disulfide linkages
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
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96% of acrosin of capacitated sperm samples and control is present in the zymogen form
proteolytic modification
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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
side-chain modification
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glycoprotein
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
side-chain modification
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glycoprotein
proteolytic modification
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the inactive form proacrosin needs to be activated to acrosin autocatalytically during the acrosome reaction
side-chain modification
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glycoprotein
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3
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stable, destruction at alkaline pH
36469
4
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above pH 4 conversion of alpha-form to beta-form
36460
4
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4C, partially purified enzyme, stable
36468
5.5
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presence of 0.1% Triton X-100
36463
8.1
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4C, 60% loss of activity after 2 min
36468
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
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10 min, 50% loss of activity
36469
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
lyophilization, unstable
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ultrafiltration, unstable
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no differences are found in the enzyme activity of sperm suspension in fresh and frozen-thawed semen
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Ca2+ stabilizes
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freeze-drying: beta-acrosin: very stable
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more, psi-acrosin: unstable
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Ca2+ stabilizes
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freeze-drying: beta-acrosin: inactivates
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freezing inactivates
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urea inactivates
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, pH 3.2, 0.5 M KCl, stable for weeks
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4C, 3 weeks, 5-10% loss of activity
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4C, lyophilized, no loss of activity for 2 years
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proacrosin
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BioSep-SEC-S2000 column chromatography, BioBasic 8 column chromatography, and Superdex 200 gel filtration
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BioSep-SEC-S2000 gel filtration, BioBasic 8 column chromatography, and Superdex 200 gel filtration
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Superdex 200 gel filtration
partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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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
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use of total enzyme activity as biochemical marker for clinical evaluation of unexplained infertility in males
medicine
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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
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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
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possible use as parameter for the determination of infertility
medicine
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acrosin represents a potential target for the design and development of male contraceptive agents