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 ACCESSION NO.
LITERATURE
preferential cleavage: Arg-/-, Lys-/-
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
endopeptidase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
53 kDa fucose-binding protein
-
-
-
-
acrosin
B0LM06
trypsin-like serine protease of the S1 family
acrosin
P79343
trypsin-like serine protease of the S1 family
acrosin
B0LM16
trypsin-like serine protease of the S1 family
acrosin
-
trypsin-like serine protease of the S1 family
acrosin
Q60491
trypsin-like serine protease of the S1 family
acrosin
B0LM30
trypsin-like serine protease of the S1 family
acrosin
B0LM26
trypsin-like serine protease of the S1 family
acrosin
B0LM13
trypsin-like serine protease of the S1 family
acrosin
B0LM07
trypsin-like serine protease of the S1 family
acrosin
B0LM09
trypsin-like serine protease of the S1 family
acrosin
B0LM10
trypsin-like serine protease of the S1 family
acrosin
B0LM27
trypsin-like serine protease of the S1 family
acrosin
B0LM36
trypsin-like serine protease of the S1 family
acrosin
B0LM17
trypsin-like serine protease of the S1 family
acrosin
B0LM18
trypsin-like serine protease of the S1 family
acrosin
P10323
trypsin-like serine protease of the S1 family
acrosin
B0LM35
trypsin-like serine protease of the S1 family
acrosin
B0LM21
trypsin-like serine protease of the S1 family
acrosin
B0LM12
trypsin-like serine protease of the S1 family
acrosin
-
trypsin-like serine protease of the S1 family
acrosin
B0LM11
trypsin-like serine protease of the S1 family
acrosin
B0LM29
trypsin-like serine protease of the S1 family
acrosin
Q3ZB05
trypsin-like serine protease of the S1 family
acrosin
B0LM32
trypsin-like serine protease of the S1 family
acrosin
B0LM15
trypsin-like serine protease of the S1 family
acrosin
P48038
trypsin-like serine protease of the S1 family
acrosin
B0LM38
trypsin-like serine protease of the S1 family
acrosin
Q9GL10
trypsin-like serine protease of the S1 family
acrosin
B0LM34
trypsin-like serine protease of the S1 family
acrosin
B0LM08
trypsin-like serine protease of the S1 family
acrosin
B0LM19
trypsin-like serine protease of the S1 family
acrosin
B0LM37
trypsin-like serine protease of the S1 family
acrosin
P29293
trypsin-like serine protease of the S1 family
acrosin
B0LM24
trypsin-like serine protease of the S1 family
acrosin
P08001
trypsin-like serine protease of the S1 family
acrosin
B0LM33
trypsin-like serine protease of the S1 family
acrosin
B0LM23
trypsin-like serine protease of the S1 family
acrosin
B0LM25
trypsin-like serine protease of the S1 family
acrosin
B0LM28
trypsin-like serine protease of the S1 family
acrosin
B0LM22
trypsin-like serine protease of the S1 family
acrosin
B0LM14
trypsin-like serine protease of the S1 family
acrosin
B0LM31
trypsin-like serine protease of the S1 family
acrosin
B0LM20
trypsin-like serine protease of the S1 family
acrosin amidase
-
-
-
-
acrosin amidase
-
-
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
SEQUENCE CODE
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
B0LM13
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
-
Q3ZB05
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 ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
sperm acrosin is responsible for the sperm binding to the egg envelope (perivitelline membrane) during fertilization
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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-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 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 + 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
-
?
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
?
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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 ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activates
Ca2+
-
activates
Ca2+
-
activates
Ca2+
-
activates
Mg2+
-
activates
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
2,6-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
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-[(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-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
-
-
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
-
-
D-arabinose
-
-
D-fructose
-
-
dacarbazine
-
BIC
diisopropylfluorophosphate
-
weak
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
dithiothreitol
-
-
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 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-(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-[(3-chloropropanoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(4-benzylbenzoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(phenylcarbonyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(trifluoroacetyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
human protein C inhibitor
-
-
-
iodoacetate
-
-
Kazal seminal plasma inhibitor
Q2UVH8
-
-
L-arginine
-
esterolytic activity
L-histidine
-
weak
L-Homoarginine
-
-
Leupeptin
-
-
methyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
N,N-dibenzyl-2-[4-(propan-2-ylsulfamoyl)phenoxy]acetamide
-
-
N-(4-chlorophenyl)-N-[2-[(2E)-2-(3-methoxy-4-methylbenzylidene)hydrazinyl]-2-oxoethyl]benzenesulfonamide (non-preferred name)
-
-
N-alpha-tosyl-L-lysyl-chloromethylketone
-
-
N-cyclohexyl-2-[(4,6-diphenylpyrimidin-2-yl)sulfanyl]acetamide
-
-
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
-
-
-
NSC651015
-
-
NSC651016
-
-
ovomucoid
-
chicken
-
ovomucoid
-
-
-
ovomucoid
-
-
-
p-aminobenzamidine
-
-
p-aminobenzamidine
-
-
p-hydroxymercuribenzoate
-
-
phenylmethylsulfonyl fluoride
-
-
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
-
-
-
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 4-methyl-3-([4-[(2-methylbenzyl)(methylsulfonyl)amino]benzoyl]amino)benzoate
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
progesterone
-
up to 2fold activation
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
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
115
162
Nalpha-benzoyl-L-Arg ethyl ester
-
-
49
-
toluene-p-sulfonyl-L-arginine methyl ester hydrochloride
-
-
-
320
-
aminobenzoyl-Ser-Lys-Gly-Arg-Ser-Leu-Ile-Gly-Lys(dinitrophenyl)-Asp
-
pH 7.4, 37C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.28
-
3-(4-nitrophenyl)isoxazole-5-carbaldehyde
-
pH 8.0, 37C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00563
-
2,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
pH and temperature not specified in the publication
0.00596
-
2,6-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
pH and temperature not specified in the publication
0.00935
-
2-(4-chlorophenoxy)-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]acetamide
-
pH and temperature not specified in the publication
0.00763
-
2-bromo-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
pH and temperature not specified in the publication
0.0063
-
2-chloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
pH and temperature not specified in the publication
0.0038
-
3,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
pH and temperature not specified in the publication
0.42
-
3-(4-nitrophenyl)-1,2-oxazole-5-carbaldehyde
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
0.007
-
3-chloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
pH and temperature not specified in the publication
0.00251
-
3-methylbutyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
pH and temperature not specified in the publication
0.0033
-
3-[4-([[4-(aminomethyl)cyclohexyl]carbonyl]oxy)phenyl]propanoic acid
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
0.008
-
4-(acetylamino)phenyl 4-carbamimidamidobenzoate
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
0.00384
-
4-(chloromethyl)-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
pH and temperature not specified in the publication
0.00925
-
4-([4-[3-(ethoxycarbonyl)-1H-pyrazol-5-yl]phenyl]amino)-4-oxobutanoic acid
-
pH and temperature not specified in the publication
0.3447
-
4-[(2-methylbenzyl)(methylsulfonyl)amino]-N-(pyridin-4-ylmethyl)benzamide
-
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
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
0.0174
-
5-([4-[3-(ethoxycarbonyl)-1H-pyrazol-5-yl]phenyl]amino)-5-oxopentanoic acid
-
pH and temperature not specified in the publication
0.0095
-
butyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
pH and temperature not specified in the publication
0.00221
-
ethyl 1-(phenylcarbonyl)-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
pH and temperature not specified in the publication
0.00029
-
ethyl 1-[(2,4-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
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
-
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
-
pH and temperature not specified in the publication
0.00299
-
ethyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
pH and temperature not specified in the publication
0.00044
-
ethyl 5-(4-[[(2,4-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.0048
-
ethyl 5-(4-[[(2,6-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.00398
-
ethyl 5-(4-[[(2,6-difluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.0024
-
ethyl 5-(4-[[(2-bromophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.00011
-
ethyl 5-(4-[[(2-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.00331
-
ethyl 5-(4-[[(4-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.0024
-
ethyl 5-(4-[[(4-fluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.0008
-
ethyl 5-(4-[[(4-methoxyphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.0346
-
ethyl 5-(4-[[(4-methylphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.0033
-
ethyl 5-(4-[[4-(1-phenylpropyl)benzoyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.023
-
ethyl 5-[4-(acetylamino)phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.017
-
ethyl 5-[4-(butanoylamino)phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.072
-
ethyl 5-[4-(pentanoylamino)phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.014
-
ethyl 5-[4-(propanoylamino)phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
3.2e-05
-
ethyl 5-[4-([4-[(4-methylphenyl)sulfonyl]benzoyl]amino)phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.00331
-
ethyl 5-[4-([[4-(chloromethyl)phenyl]carbonyl]amino)phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.00576
-
ethyl 5-[4-[(3-chloropropanoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.00047
-
ethyl 5-[4-[(4-benzylbenzoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.008
-
ethyl 5-[4-[(phenylcarbonyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
0.0079
-
ethyl 5-[4-[(trifluoroacetyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
pH and temperature not specified in the publication
2.7e-05
-
KF950
-
pH and temperature not specified in the publication
0.0093
-
methyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
pH and temperature not specified in the publication
0.1555
-
methyl 4-methyl-3-([4-[(2-methylbenzyl)(methylsulfonyl)amino]benzoyl]amino)benzoate
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
0.4267
-
N,N-dibenzyl-2-[4-(propan-2-ylsulfamoyl)phenoxy]acetamide
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
0.014
-
N-(4-chlorophenyl)-N-[2-[(2E)-2-(3-methoxy-4-methylbenzylidene)hydrazinyl]-2-oxoethyl]benzenesulfonamide (non-preferred name)
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
0.1426
-
N-alpha-tosyl-L-lysyl-chloromethylketone
-
pH and temperature not specified in the publication
0.1426
-
N-alpha-tosyl-L-lysyl-chloromethylketone
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
0.3551
-
N-cyclohexyl-2-[(4,6-diphenylpyrimidin-2-yl)sulfanyl]acetamide
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37C
0.1426
-
N-tosyl-L-lysine chloromethylketone
-
pH and temperature not specified in the publication
0.3018
-
N-[4-(dipropylsulfamoyl)phenyl]-3,4-diethoxybenzamide
-
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
-
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
-
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
-
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
-
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
-
pH and temperature not specified in the publication
0.00718
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2,6-difluorobenzamide
-
pH and temperature not specified in the publication
0.0093
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylphenoxy)acetamide
-
pH and temperature not specified in the publication
0.0099
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylpiperidin-1-yl)acetamide
-
pH and temperature not specified in the publication
0.00892
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(3-methylphenoxy)acetamide
-
pH and temperature not specified in the publication
0.00984
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methoxyphenoxy)acetamide
-
pH and temperature not specified in the publication
0.00898
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylphenoxy)acetamide
-
pH and temperature not specified in the publication
0.00498
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylpiperidin-1-yl)acetamide
-
pH and temperature not specified in the publication
0.0042
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-nitrophenoxy)acetamide
-
pH and temperature not specified in the publication
0.00741
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(piperidin-1-yl)acetamide
-
pH and temperature not specified in the publication
0.0023
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-phenoxyacetamide
-
pH and temperature not specified in the publication
0.0025
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3,5-dinitrobenzamide
-
pH and temperature not specified in the publication
0.00705
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3-(trifluoromethyl)benzamide
-
pH and temperature not specified in the publication
0.00013
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethoxybenzamide
-
pH and temperature not specified in the publication
0.00021
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethylbenzamide
-
pH and temperature not specified in the publication
0.00711
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-fluorobenzamide
-
pH and temperature not specified in the publication
0.00221
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methoxybenzamide
-
pH and temperature not specified in the publication
0.00206
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methylbenzamide
-
pH and temperature not specified in the publication
0.00958
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]butanamide
-
pH and temperature not specified in the publication
0.00158
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]pentanamide
-
pH and temperature not specified in the publication
0.009
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]propanamide
-
pH and temperature not specified in the publication
0.012
-
NF064
-
23C
0.7
-
NSC651015
-
23C
0.7
-
NSC651016
-
23C
0.00235
-
propan-2-yl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
pH and temperature not specified in the publication
0.00331
-
propyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
pH and temperature not specified in the publication
0.1
-
suramin
-
23C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
12
-
-
-
37
-
-
-
49.23
-
-
-
92.9
-
-
-
150
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8.5
-
-
7.7
-
-
-
7.8
-
-
-
7.8
-
-
assay at
8
-
-
assay at
8.2
-
-
-
8.5
-
-
-
8.7
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temperature
37
-
-
assay at
53
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
65
-
about 15% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.4
-
Q2UVH8
isoelectric focusing
7.3
-
Q2UVH8
mature protein, calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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
B0LM06
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
P79343
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
B0LM16
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
Q60491
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
B0LM30
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
B0LM26
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
B0LM13
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
B0LM07
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
B0LM09
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
B0LM10
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
B0LM27
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
B0LM36
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
B0LM17
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
B0LM18
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
P10323
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
B0LM35
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
B0LM21
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
B0LM12
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
B0LM11
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
B0LM29
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
Q3ZB05
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
B0LM32
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
B0LM15
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
P48038
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
B0LM38
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
Q9GL10
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
B0LM34
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
B0LM08
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
B0LM19
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
B0LM37
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
P29293
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
B0LM24
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
P08001
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
B0LM33
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
B0LM23
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
B0LM25
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
B0LM28
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
B0LM22
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
B0LM14
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
B0LM31
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
B0LM20
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
-
Manually annotated by BRENDA team
-
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 ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Acipenser ruthenus 1758
-
-
-
-
Manually annotated by BRENDA team
Acipenser ruthenus 1758
-
-
-
Manually annotated by BRENDA team
additional information
-
enzyme subcellular localization analysis, overview
-
Manually annotated by BRENDA team
additional information
Acipenser ruthenus 1758
-
enzyme subcellular localization analysis, overview
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
-
gel filtration
76000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 52000, x * 68000, x * 34000, SDS-PAGE, 3 forms with different molecular weight
?
-
x * 34500, SDS-PAGE, beta-acrosin; x * 48000, SDS-PAGE, alpha-acrosin
?
-
x * 39000, SDS-PAGE
?
-
x * 49000, SDS-PAGE
?
-
x * 38000, SDS-PAGE, beta-acrosin
?
-
x * 38000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
?
-
x * 27000, SDS-PAGE
?
-
x * 58000-60000, SDS-PAGE, doublet
?
-
x * 52000-54000, SDS-PAGE, doublet
?
-
x * 55000-59000, SDS-PAGE, doublet
?
B0LM06
x * 30469, calculated from the deduced amino acid sequence
?
P79343
x * 41722, calculated from the deduced amino acid sequence
?
B0LM16
x * 30066, calculated from the deduced amino acid sequence
?
Q60491
x * 45773, calculated from the deduced amino acid sequence
?
B0LM30
x * 25649, calculated from the deduced amino acid sequence
?
B0LM26
x * 30707, calculated from the deduced amino acid sequence
?
B0LM13
x * 30515, calculated from the deduced amino acid sequence
?
B0LM07
x * 28794, calculated from the deduced amino acid sequence
?
B0LM09
x * 30616, calculated from the deduced amino acid sequence
?
B0LM10
x * 30809, calculated from the deduced amino acid sequence
?
B0LM27
x * 30679, calculated from the deduced amino acid sequence
?
B0LM36
x * 30361, calculated from the deduced amino acid sequence
?
B0LM17
x * 26300, calculated from the deduced amino acid sequence
?
B0LM18
x * 30583, calculated from the deduced amino acid sequence
?
P10323
x * 45847, calculated from the deduced amino acid sequence
?
B0LM35
x * 30413, calculated from the deduced amino acid sequence
?
B0LM21
x * 30276, calculated from the deduced amino acid sequence
?
B0LM12
x * 30357, calculated from the deduced amino acid sequence
?
B0LM11
x * 30628, calculated from the deduced amino acid sequence
?
B0LM29
x * 26896, calculated from the deduced amino acid sequence
?
Q3ZB05
x * 43016, calculated from the deduced amino acid sequence
?
B0LM32
x * 30310, calculated from the deduced amino acid sequence
?
B0LM15
x * 28582, calculated from the deduced amino acid sequence
?
P48038
x * 46422, calculated from the deduced amino acid sequence
?
B0LM38
x * 30604, calculated from the deduced amino acid sequence
?
Q9GL10
x * 36119, calculated from the deduced amino acid sequence
?
B0LM08
x * 30233, calculated from the deduced amino acid sequence
?
B0LM19
x * 30583, calculated from the deduced amino acid sequence
?
B0LM37
x * 30455, calculated from the deduced amino acid sequence
?
P29293
x * 48623, calculated from the deduced amino acid sequence
?
B0LM24
x * 26746, calculated from the deduced amino acid sequence
?
B0LM33
x * 30534, calculated from the deduced amino acid sequence
?
B0LM23
x * 30138, calculated from the deduced amino acid sequence
?
B0LM25
x * 30202, calculated from the deduced amino acid sequence
?
B0LM28
x * 30788, calculated from the deduced amino acid sequence
?
B0LM22
x * 29689, calculated from the deduced amino acid sequence
?
B0LM14
x * 30556, calculated from the deduced amino acid sequence
?
B0LM31
x * 30452, calculated from the deduced amino acid sequence
?
B0LM20
x * 28577, calculated from the deduced amino acid sequence
?
-
x * 40000, proacrosin, SDS-PAGE, x * 32000, alpha-acrosin, SDS-PAGE, x * 27000, beta-acrosin, SDS-PAGE
?
Q2UVH8
x * 30000, active enzyme, SDS-PAGE; x * 30874, mass spectrometry; x * 360517, mature protein, calculated from amino acid sequence
?
-
x * 45000, SDS-PAGE
monomer
-
1 * 76000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
additional information
-
interaction of protein with zona pellucida glycoproteins, highest binding activity toward glycoprotein ZPA
additional information
-
proenzyme binds to bovine serum albumin-mannose, binding sites are stabilized by noncovalent bonds and disulfide linkages
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
96% of acrosin of capacitated sperm samples and control is present in the zymogen form
proteolytic modification
-
acrosin is an acrosomal protease synthesized as an inactive precursor, proacrosin, which is processed via autoproteolysis into active forms alpha- and beta-acrosin, which occurs earlier in frozen/thawed dog spermatozoa than in fresh dog spermatozoa
side-chain modification
-
glycoprotein
glycoprotein
Q2UVH8
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
-
glycoprotein
proteolytic modification
-
the inactive form proacrosin needs to be activated to acrosin autocatalytically during the acrosome reaction
side-chain modification
-
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q9GL10
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
P08001
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
-
-
stable, destruction at alkaline pH
4
-
-
above pH 4 conversion of alpha-form to beta-form
4
-
-
4C, partially purified enzyme, stable
5.5
-
-
presence of 0.1% Triton X-100
8.1
-
-
4C, 60% loss of activity after 2 min
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55
-
-
10 min, 50% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
lyophilization, unstable
-
ultrafiltration, unstable
-
Ca2+ stabilizes
-
freeze-drying: beta-acrosin: very stable
-
more, psi-acrosin: unstable
-
Ca2+ stabilizes
-
freeze-drying: beta-acrosin: inactivates
-
freezing inactivates
-
urea inactivates
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, pH 3.2, 0.5 M KCl, stable for weeks
-
4C, 3 weeks, 5-10% loss of activity
-
4C, lyophilized, no loss of activity for 2 years
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
proacrosin
-
Superdex 200 gel filtration
Q2UVH8
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
bacterial recombinant human proacrosin/acrosin proteins: Rec-40, residues 1-402, Rec-30, N-terminal fragments 1-300, Rec-20, 1-190, and Rec-10, 1-160
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
acrosin activity positively correlates with normal sperm morphology and with fertilization rate. Use of enzyme assay to predict sperm fertilizing capacity in in vitro fertilization independently of sperm morphology
medicine
-
use of total enzyme activity as biochemical marker for clinical evaluation of unexplained infertility in males
medicine
-
sperm-egg interaction: interaction of protein with zona pellucida glycoproteins, highest binding activity with glycoprotein ZPA. Interaction involves mannosyl, fucosyl, and sulfated glycans. Binding sites are located both on N- and C-terminus of proacrosin, revealing a key role of proenzyme in the interaction
medicine
-
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
-
possible use as parameter for the determination of infertility
medicine
-
acrosin represents a potential target for the design and development of male contraceptive agents