Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
aminobenzoyl-Ser-Lys-Gly-Arg-Ser-Leu-Ile-Gly-Lys(dinitrophenyl)-Asp + H2O
?
-
-
-
?
collagen I + H2O
?
-
heat denatured
-
-
?
Collagen IV + H2O
?
-
-
-
-
?
D-valyl-L-leucyl-L-arginine p-nitroanilide + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
N-benzoyl-DL-arginine-p-nitroanilide + H2O
?
-
-
-
-
?
Nalpha-benzoyl-DL-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
Nalpha-benzoyl-DL-arginine-p-nitroanilide + H2O
?
-
-
-
-
?
Nalpha-benzoyl-DL-arginyl-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-lysine p-nitroanilide + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide hydrochloride + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine beta-naphthylamide + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
Nalpha-benzoyl-L-arginine ethyl ester hydrochloride + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine p-nitroanilide + H2O
?
Nalpha-tosyl-L-arginine methyl ester + H2O
?
proacrosin + H2O
acrosin + ?
proacrosin + H2O
acrosin + peptide
proteinase-activated receptor-2 + H2O
?
toluene-p-sufonyl-L-arginine methyl ester + H2O
?
-
-
-
-
?
toluene-p-sulfonyl-L-arginine methyl ester + H2O
?
-
-
-
-
?
additional information
?
-
Nalpha-benzoyl-DL-arginine 4-nitroanilide + H2O

Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O

Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O

?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine p-nitroanilide + H2O

?
-
-
-
-
?
Nalpha-benzoyl-L-arginine p-nitroanilide + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-arginine p-nitroanilide + H2O
?
-
-
-
-
?
Nalpha-tosyl-L-arginine methyl ester + H2O

?
-
-
-
-
?
Nalpha-tosyl-L-arginine methyl ester + H2O
?
-
-
-
-
?
proacrosin + H2O

acrosin + ?
-
-
-
-
?
proacrosin + H2O
acrosin + ?
-
-
-
-
?
proacrosin + H2O

acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
-
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
-
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proteinase-activated receptor-2 + H2O

?
-
-
-
?
proteinase-activated receptor-2 + H2O
?
-
the enzyme may play additional role(s) in the fertilization process via the activation of PAR-2 on oocytes
-
?
additional information

?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
possibly important for fertilization process, involved in the acrosome reaction, binding of spermatozoa to and penetration through the zona pellucida
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
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
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
proacrosin + H2O
acrosin + ?
proacrosin + H2O
acrosin + peptide
proteinase-activated receptor-2 + H2O
?
-
the enzyme may play additional role(s) in the fertilization process via the activation of PAR-2 on oocytes
-
?
additional information
?
-
proacrosin + H2O

acrosin + ?
-
-
-
-
?
proacrosin + H2O
acrosin + ?
-
-
-
-
?
proacrosin + H2O

acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
-
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
-
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
proacrosin + H2O
acrosin + peptide
acrosin autoactivates through an endoproteolytic cleavage at the N-terminus with subsequent conversion to the mature enzyme through C-terminus cleavages
-
-
?
additional information

?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
possibly important for fertilization process, involved in the acrosome reaction, binding of spermatozoa to and penetration through the zona pellucida
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
-
digestion of zona pellucida by sperm, glycoprotein layer surrounding the oocyte
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
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
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
additional information
?
-
lysis of Arg/Lys-X bonds
-
-
?
additional information
?
-
thought to fulfill several different roles in fertilization including that of a serine protease and in secondary zona pellucida binding
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-(2,4-dichlorobenzoyl)-N-methyl-1H-indazole-3-carboxamide
-
-
2,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
2,6-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
-
-
2-(3-(2-hydroxyethyl)ureido)-N-(2-methoxybenzyl)-1H-benzo[d]imidazole-5-sulfonamide
-
-
2-(3-(2-hydroxyethyl)ureido)-N-(2-methylbenzyl)-1H-benzo[d]imidazole-5-sulfonamide
-
-
2-(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-{[(2-hydroxyethyl)carbamoyl]amino}-N-[(2-methoxyphenyl)methyl]-1H-benzimidazole-5-sulfonamide
-
-
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-(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-carbomethoxyphenyl 4-guanidinobenzoate mesylate
-
4'-CMGB, a sperm acrosin inhibitor and candidate for an vaginal contraceptive drug. Method development and evaluation of 4'-CMGB identification and activity determination involving HPLC and LC-tandem mass spectrometry, overview
4-nitrophenyl 4-carbamimidamidobenzoate
-
-
4-nitrophenyl 4-guanidinobenzoate
-
-
4-[(2-methylbenzyl)(methylsulfonyl)amino]-N-(pyridin-4-ylmethyl)benzamide
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5-(2,4-dichlorophenyl)-1,2-oxazole-3-carbaldehyde
-
-
5-(2,4-dichlorophenyl)isoxazole-3-carbaldehyde
-
50% inhibition at 0.39 mM, weak antifungal activity against Candida albicans
5-(2-chlorophenyl)isoxazole-3-carbaldehyde
-
50% inhibition at 1.0 mM, weak antifungal activity against Candida albicans
5-(3-bromophenyl)isoxazole-3-carbaldehyde
-
50% inhibition at 1.1 mM, weak antifungal activity against Candida albicans
5-(4-carbamimidamidophenyl)-N-(1-hydroxypropan-2-yl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2,3-dimethylphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2,4-dimethoxyphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2,5-dimethoxyphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2,6-dimethylphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2-methoxyphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(2-methylphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(3,5-dimethylphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(3-chlorophenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(3-methoxyphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(3-methylphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(4-chlorophenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(4-cyanophenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(4-ethoxyphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(4-fluorophenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(4-methylphenyl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(4-methylpyridin-2-yl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(naphthalen-1-yl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-(propan-2-yl)-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-phenyl-1,2-oxazole-3-carboxamide
-
-
5-(4-carbamimidamidophenyl)-N-[4-(trifluoromethyl)phenyl]-1,2-oxazole-3-carboxamide hydrochloride
-
-
5-(4-methylphenyl)isoxazole-3-carbaldehyde
-
50% inhibition at 2.4 mM, weak antifungal activity against Candida albicans
5-([4-[3-(ethoxycarbonyl)-1H-pyrazol-5-yl]phenyl]amino)-5-oxopentanoic acid
-
-
5-phenylisoxazole-3-carbaldehyde
-
50% inhibition at 2.4 mM, weak antifungal activity against Candida albicans
7-amino-1-chloro-3-L-tosylamidoheptan-2-one
-
weak
Benzamidine hydrochloride
-
50% inhibition at 2.2 mM, weak antifungal activity against Candida albicans
butyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
diisopropylfluorophosphate
ethyl 1-(2,4-dichlorobenzoyl)-1H-indazole-3-carboxylate
-
-
ethyl 1-(phenylcarbonyl)-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-(thiophen-2-ylcarbonyl)-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2,4-dichlorophenyl)acetyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2,4-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2,4-dimethoxyphenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2,6-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-bromo-4-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-chloro-4-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
most potent inhibitor
ethyl 1-[(2-chlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-methoxyphenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(2-methylphenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(3,4-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[(3-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
-
-
ethyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
ethyl 4-([[5-(4-carbamimidamidophenyl)-1,2-oxazol-3-yl]carbonyl]amino)benzoate hydrochloride
-
-
ethyl 5-(4-[[(2,4-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(2,6-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(2,6-difluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(2-bromophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(2-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(4-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(4-fluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(4-methoxyphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[(4-methylphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-(4-[[4-(1-phenylpropyl)benzoyl]amino]phenyl)-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-(acetylamino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-(benzoylamino)phenyl]-1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-(butanoylamino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-(pentanoylamino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-(propanoylamino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-([4-[(4-methylphenyl)sulfonyl]benzoyl]amino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-([[4-(chloromethyl)phenyl]carbonyl]amino)phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(2-chlorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-[(3,4-dichlorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-[(3-chloropropanoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(4-benzylbenzoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(4-chlorobenzoyl)amino]phenyl]1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-[(4-fluorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
-
-
ethyl 5-[4-[(phenylcarbonyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
ethyl 5-[4-[(trifluoroacetyl)amino]phenyl]-1H-pyrazole-3-carboxylate
-
-
guanidinobenzoate
-
KF950
human protein C inhibitor
-
-
-
Kazal seminal plasma inhibitor
-
-
L-1-chloro-3-[4-tosylamido]-7-amino-2-heptanone
-
-
L-arginine
-
esterolytic activity
methyl (6-[[4-(trifluoromethyl)phenyl]sulfamoyl]-1H-benzimidazol-2-yl)carbamate
-
-
methyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
-
-
methyl 4-methyl-3-([4-[(2-methylbenzyl)(methylsulfonyl)amino]benzoyl]amino)benzoate
-
-
methyl [6-(butylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-(hexylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-(phenylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-(propan-2-ylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2,5-dimethylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(2-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3,4-dimethoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(3-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-bromophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[(4-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[benzyl(methyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
methyl [6-[bis(3-methylbutyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
-
-
N,N-bis(2-hydroxyethyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
-
-
N,N-dibenzyl-2-[4-(propan-2-ylsulfamoyl)phenoxy]acetamide
-
-
N-(2-bromophenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide
-
-
N-(2-chlorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-(2-fluorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-(2-hydroxyethyl)-5-(4-methoxyphenyl)-N-methyl-1H-pyrazole-3-carboxamide
-
-
N-(2-hydroxypropyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
-
-
N-(3, 5-difluorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-(3,5-dichlorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-(3-bromophenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
N-(3-hydroxypropyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
-
-
N-(4-chlorophenyl)-N-[2-[(2E)-2-(3-methoxy-4-methylbenzylidene)hydrazinyl]-2-oxoethyl]benzenesulfonamide (non-preferred name)
-
-
N-(4-tert-butylphenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
-
-
N-(5-bromobenzo[d]thiazol-2-yl)-2-(4-pentylpiperazin-1-yl)acetamide
-
-
N-(5-bromobenzo[d]thiazol-2-yl)-2-(diisopentylamino)acetamide
-
-
N-(5-bromobenzo[d]thiazol-2-yl)-2-(dipentylamino)acetamide
-
-
N-(6-bromobenzo[d]thiazol-2-yl)-2-(dibutylamino)acetamide
-
-
N-(diaminomethylidene)-4-(4-methylanilino)benzene-1-sulfonamide
-
-
N-alpha-tosyl-L-lysyl-chloromethyl-ketone
-
-
N-alpha-tosyl-L-lysyl-chloromethylketone
-
-
N-benzyl-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-cyclohexyl-2-[(4,6-diphenylpyrimidin-2-yl)sulfanyl]acetamide
-
-
N-hexyl-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
-
-
N-tosyl-L-lysine chloromethylketone
-
-
N-[4-(dipropylsulfamoyl)phenyl]-3,4-diethoxybenzamide
-
-
N-[4-[(4-benzylpiperazin-1-yl)carbonyl]phenyl]-2,3,5,6-tetramethylbenzenesulfonamide
-
-
N-[4-[(4-benzylpiperazin-1-yl)carbonyl]phenyl]-4-tert-butylbenzenesulfonamide
-
-
N-[4-[(4-fluorophenyl)sulfamoyl]phenyl]-3,4,5-trimethoxybenzamide
-
-
N-[4-[(4-methoxyphenyl)sulfamoyl]phenyl]-2-(naphthalen-1-yloxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2,4,6-trimethylbenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2,6-difluorobenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylphenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylpiperidin-1-yl)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(3-methylphenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methoxyphenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylphenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylpiperidin-1-yl)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-nitrophenoxy)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(piperidin-1-yl)acetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-phenoxyacetamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3,5-dinitrobenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3-(trifluoromethyl)benzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethoxybenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethylbenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-fluorobenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methoxybenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methylbenzamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]butanamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]pentanamide
-
-
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]propanamide
-
-
Nalpha-benzoyl-DL-arginine p-nitroanilide
-
-
Nalpha-tosyl-L-lysine chloromethyl ketone
Nalpha-tosyl-L-phenylalanyl-chloromethane
-
-
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
-
Trypsin inhibitor II
-
-
-
Trypsin-plasmin inhibitor
-
bdellin B-3
-
antithrombin

-
-
-
Aprotinin

-
-
benzamidine

-
-
diisopropylfluorophosphate

-
weak
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
Hg2+

-
-
iodoacetate

-
-
leupeptin

-
-
Nalpha-tosyl-L-lysine chloromethyl ketone

-
-
Nalpha-tosyl-L-lysine chloromethyl ketone
-
-
Nalpha-tosyl-L-lysine chloromethyl ketone
-
-
Nalpha-tosyl-L-lysine chloromethyl ketone
-
-
ovomucoid

-
-
-
p-aminobenzamidine

-
-
suramin

-
-
suramin
-
compound with combined antifertility agent and microbicide, three to four molecules of suramin bind to one molecule of enzyme
suramin
-
compound with combined antifertility agent and microbicide, three to four molecules of suramin bind to one molecule of enzyme
Trypsin inhibitor

-
soybean
-
Trypsin inhibitor
-
soybean
-
Trypsin inhibitor
-
bovine pancreatic; lima-bean; soybean
-
Trypsin inhibitor
-
lima-bean
-
Trypsin inhibitor
-
soybean
-
Trypsin inhibitor
-
soybean
-
Zn2+

-
-
additional information

-
inhibited by naturally occuring trypsin inhibitors, esterolytic activity, competitively inhibited by L-arginine but not by L-lysine
-
additional information
-
inhibited by naturally occuring trypsin inhibitors, esterolytic activity, competitively inhibited by L-arginine but not by L-lysine; nearly all trypsin inhibitors
-
additional information
-
inhibited by naturally occuring trypsin inhibitors, esterolytic activity, competitively inhibited by L-arginine but not by L-lysine
-
additional information
-
inhibited by naturally occuring trypsin inhibitors, esterolytic activity, competitively inhibited by L-arginine but not by L-lysine
-
additional information
-
mechanism of inhibition
-
additional information
-
no inhibition with quercetin-3beta-D-glucoside or quercetin-3beta-D-glucoside sulfate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3.78
1-(2,4-dichlorobenzoyl)-N-methyl-1H-indazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00563
2,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00596
2,6-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
6.04
2-(3-(2-hydroxyethyl)ureido)-N-(2-methoxybenzyl)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
5.45
2-(3-(2-hydroxyethyl)ureido)-N-(2-methylbenzyl)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00935
2-(4-chlorophenoxy)-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00763
2-bromo-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0063
2-chloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
7.32
2-{[(2-hydroxyethyl)carbamoyl]amino}-N-[(2-methoxyphenyl)methyl]-1H-benzimidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0038
3,4-dichloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.42
3-(4-nitrophenyl)-1,2-oxazole-5-carbaldehyde
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.007
3-chloro-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00251
3-methylbutyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0033
3-[4-([[4-(aminomethyl)cyclohexyl]carbonyl]oxy)phenyl]propanoic acid
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.008
4-(acetylamino)phenyl 4-carbamimidamidobenzoate
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.00384
4-(chloromethyl)-N-[4-[(diaminomethylidene)sulfamoyl]phenyl]benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00925
4-([4-[3-(ethoxycarbonyl)-1H-pyrazol-5-yl]phenyl]amino)-4-oxobutanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.3447
4-[(2-methylbenzyl)(methylsulfonyl)amino]-N-(pyridin-4-ylmethyl)benzamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.39 - 1.7
5-(2,4-dichlorophenyl)-1,2-oxazole-3-carbaldehyde
0.1
5-(4-carbamimidamidophenyl)-N-(1-hydroxypropan-2-yl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0115
5-(4-carbamimidamidophenyl)-N-(2,3-dimethylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0014
5-(4-carbamimidamidophenyl)-N-(2,4-dimethoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0023
5-(4-carbamimidamidophenyl)-N-(2,5-dimethoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0057
5-(4-carbamimidamidophenyl)-N-(2,6-dimethylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0084
5-(4-carbamimidamidophenyl)-N-(2-methoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0144
5-(4-carbamimidamidophenyl)-N-(2-methylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0121
5-(4-carbamimidamidophenyl)-N-(3,5-dimethylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0254
5-(4-carbamimidamidophenyl)-N-(3-chlorophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0066
5-(4-carbamimidamidophenyl)-N-(3-methoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0094
5-(4-carbamimidamidophenyl)-N-(3-methylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0268
5-(4-carbamimidamidophenyl)-N-(4-chlorophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0239
5-(4-carbamimidamidophenyl)-N-(4-cyanophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0064
5-(4-carbamimidamidophenyl)-N-(4-ethoxyphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0205
5-(4-carbamimidamidophenyl)-N-(4-fluorophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0101
5-(4-carbamimidamidophenyl)-N-(4-methylphenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0214
5-(4-carbamimidamidophenyl)-N-(4-methylpyridin-2-yl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0299
5-(4-carbamimidamidophenyl)-N-(naphthalen-1-yl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.1
5-(4-carbamimidamidophenyl)-N-(propan-2-yl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0246
5-(4-carbamimidamidophenyl)-N-phenyl-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
0.0203
5-(4-carbamimidamidophenyl)-N-[4-(trifluoromethyl)phenyl]-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8ưC
0.0174
5-([4-[3-(ethoxycarbonyl)-1H-pyrazol-5-yl]phenyl]amino)-5-oxopentanoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0095
butyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
3.24
ethyl 1-(2,4-dichlorobenzoyl)-1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00221
ethyl 1-(phenylcarbonyl)-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00029
ethyl 1-[(2,4-dichlorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00174
ethyl 1-[(2-bromo-4-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00347
ethyl 1-[(2-chloro-4-fluorophenyl)carbonyl]-1H-pyrrolo[2,3-b]pyridine-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00299
ethyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0093
ethyl 4-([[5-(4-carbamimidamidophenyl)-1,2-oxazol-3-yl]carbonyl]amino)benzoate hydrochloride
Homo sapiens
-
pH 7.8, 37.8ưC
0.00044
ethyl 5-(4-[[(2,4-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0048
ethyl 5-(4-[[(2,6-dichlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00398
ethyl 5-(4-[[(2,6-difluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0024
ethyl 5-(4-[[(2-bromophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00011
ethyl 5-(4-[[(2-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00331
ethyl 5-(4-[[(4-chlorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0024
ethyl 5-(4-[[(4-fluorophenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0008
ethyl 5-(4-[[(4-methoxyphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0346
ethyl 5-(4-[[(4-methylphenyl)carbonyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0033
ethyl 5-(4-[[4-(1-phenylpropyl)benzoyl]amino]phenyl)-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.023
ethyl 5-[4-(acetylamino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.46
ethyl 5-[4-(benzoylamino)phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8ưC
0.017
ethyl 5-[4-(butanoylamino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.072
ethyl 5-[4-(pentanoylamino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.014
ethyl 5-[4-(propanoylamino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000032
ethyl 5-[4-([4-[(4-methylphenyl)sulfonyl]benzoyl]amino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00331
ethyl 5-[4-([[4-(chloromethyl)phenyl]carbonyl]amino)phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.06
ethyl 5-[4-[(2-chlorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8ưC
0.24
ethyl 5-[4-[(3,4-dichlorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8ưC
0.00576
ethyl 5-[4-[(3-chloropropanoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00047
ethyl 5-[4-[(4-benzylbenzoyl)amino]phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.38
ethyl 5-[4-[(4-chlorobenzoyl)amino]phenyl]1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8ưC
0.14
ethyl 5-[4-[(4-fluorobenzoyl)amino]phenyl]-1,2-oxazole-3-carboxylate
Homo sapiens
-
pH 7.8, 37.8ưC
0.008
ethyl 5-[4-[(phenylcarbonyl)amino]phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0079
ethyl 5-[4-[(trifluoroacetyl)amino]phenyl]-1H-pyrazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.000027
KF950
Homo sapiens
-
pH and temperature not specified in the publication
10.7
methyl (6-[[4-(trifluoromethyl)phenyl]sulfamoyl]-1H-benzimidazol-2-yl)carbamate
Homo sapiens
-
pH 8.0, 22ưC
0.0093
methyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.1555
methyl 4-methyl-3-([4-[(2-methylbenzyl)(methylsulfonyl)amino]benzoyl]amino)benzoate
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
1.77
methyl [6-(butylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
1.8
methyl [6-(hexylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
1.03
methyl [6-(phenylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
0.47
methyl [6-(propan-2-ylsulfamoyl)-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
1.27
methyl [6-[(2,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
1.55
methyl [6-[(2,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
8.86
methyl [6-[(2,5-dimethylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
5.75
methyl [6-[(2-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
0.31
methyl [6-[(2-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
8.42
methyl [6-[(2-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
4.02
methyl [6-[(3,4-dichlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
1.59
methyl [6-[(3,4-difluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
11.5
methyl [6-[(3,4-dimethoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
1.81
methyl [6-[(3-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
7.5
methyl [6-[(3-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
5.06
methyl [6-[(3-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
1.64
methyl [6-[(4-bromophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
7.52
methyl [6-[(4-chlorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
2.4
methyl [6-[(4-fluorophenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
3.29
methyl [6-[(4-methoxyphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
3.18
methyl [6-[(4-methylphenyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
1.25
methyl [6-[benzyl(methyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
0.063
methyl [6-[bis(3-methylbutyl)sulfamoyl]-1H-benzimidazol-2-yl]carbamate
Homo sapiens
-
pH 8.0, 22ưC
5.73
N,N-bis(2-hydroxyethyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.4267
N,N-dibenzyl-2-[4-(propan-2-ylsulfamoyl)phenoxy]acetamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.0279
N-(2-bromophenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide
Homo sapiens
-
pH 7.8, 37.8ưC
1.06
N-(2-chlorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.08
N-(2-fluorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
6.81
N-(2-hydroxyethyl)-5-(4-methoxyphenyl)-N-methyl-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
8.92
N-(2-hydroxypropyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.34
N-(3, 5-difluorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
2.45
N-(3,5-dichlorobenzyl)-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0144
N-(3-bromophenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8ưC
1.43
N-(3-hydroxypropyl)-5-(4-methoxyphenyl)-1H-pyrazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.014
N-(4-chlorophenyl)-N-[2-[(2E)-2-(3-methoxy-4-methylbenzylidene)hydrazinyl]-2-oxoethyl]benzenesulfonamide (non-preferred name)
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.0078
N-(4-tert-butylphenyl)-5-(4-carbamimidamidophenyl)-1,2-oxazole-3-carboxamide hydrochloride
Homo sapiens
-
pH 7.8, 37.8ưC
5.08
N-(5-bromobenzo[d]thiazol-2-yl)-2-(4-pentylpiperazin-1-yl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
1.09
N-(5-bromobenzo[d]thiazol-2-yl)-2-(diisopentylamino)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.54
N-(5-bromobenzo[d]thiazol-2-yl)-2-(dipentylamino)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
2.78
N-(6-bromobenzo[d]thiazol-2-yl)-2-(dibutylamino)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
142.6
N-alpha-tosyl-L-lysyl-chloromethyl-ketone
Homo sapiens
-
pH and temperature not specified in the publication
0.1426
N-alpha-tosyl-L-lysyl-chloromethylketone
0.28
N-benzyl-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.3551
N-cyclohexyl-2-[(4,6-diphenylpyrimidin-2-yl)sulfanyl]acetamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
1.62
N-hexyl-2-(3-(2-hydroxyethyl)ureido)-1H-benzo[d]imidazole-5-sulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.1426
N-tosyl-L-lysine chloromethylketone
Homo sapiens
-
pH and temperature not specified in the publication
0.3018
N-[4-(dipropylsulfamoyl)phenyl]-3,4-diethoxybenzamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.6248
N-[4-[(4-benzylpiperazin-1-yl)carbonyl]phenyl]-2,3,5,6-tetramethylbenzenesulfonamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
3.057
N-[4-[(4-benzylpiperazin-1-yl)carbonyl]phenyl]-4-tert-butylbenzenesulfonamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.2053
N-[4-[(4-fluorophenyl)sulfamoyl]phenyl]-3,4,5-trimethoxybenzamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.6678
N-[4-[(4-methoxyphenyl)sulfamoyl]phenyl]-2-(naphthalen-1-yloxy)acetamide
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.00245
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2,4,6-trimethylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00718
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2,6-difluorobenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0093
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylphenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0099
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(2-methylpiperidin-1-yl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00892
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(3-methylphenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00984
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methoxyphenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00898
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylphenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00498
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-methylpiperidin-1-yl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0042
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(4-nitrophenoxy)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00741
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-(piperidin-1-yl)acetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0023
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-2-phenoxyacetamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0025
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3,5-dinitrobenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00705
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-3-(trifluoromethyl)benzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00013
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethoxybenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00021
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-ethylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00711
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-fluorobenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00221
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methoxybenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00206
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]-4-methylbenzamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00958
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]butanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.00158
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]pentanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.009
N-[4-[(diaminomethylidene)sulfamoyl]phenyl]propanamide
Homo sapiens
-
pH and temperature not specified in the publication
0.012
NF064
Sus scrofa
-
23ưC
0.7
NSC651015
Sus scrofa
-
23ưC
0.7
NSC651016
Sus scrofa
-
23ưC
0.00235
propan-2-yl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00331
propyl 1-[2-([4-[(diaminomethylidene)sulfamoyl]phenyl]amino)-2-oxoethyl]piperidine-4-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.1
suramin
Sus scrofa
-
23ưC
0.39
5-(2,4-dichlorophenyl)-1,2-oxazole-3-carbaldehyde

Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
0.39
5-(2,4-dichlorophenyl)-1,2-oxazole-3-carbaldehyde
Homo sapiens
-
pH 7.8, 37.8ưC
1.7
5-(2,4-dichlorophenyl)-1,2-oxazole-3-carbaldehyde
Homo sapiens
-
pH 8.0, 22ưC
0.1426
N-alpha-tosyl-L-lysyl-chloromethylketone

Homo sapiens
-
pH and temperature not specified in the publication
0.1426
N-alpha-tosyl-L-lysyl-chloromethylketone
Homo sapiens
-
in 55 mM HEPES and 55 mM NaCl at pH 8.0 and 37ưC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
36461, 36462, 36468, 36479, 668293, 668679, 668680, 668887, 692404, 753777, 755363 brenda
-
from infertile men
brenda
-
compared to control, enzyme activity is significantly lower in patients with unexplained infertility but high sperm mobility and in patients with infertility and low sperm mobility
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
the protein is distributed on the surface and in the acrosomal matrix of the sperm head
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
acrosin is a major serine proteinase of mammalian sperm
brenda
-
ultrastructure of sterlet sperm, sperm cells possess a head with a distinct acrosome, a midpiece and a single flagellum surrounded by the flagellar plasma membrane, overview. The enzyme is localized in acrosome, endonuclear canals and implantation fossa
brenda
-
ultrastructure of sterlet sperm, sperm cells possess a head with a distinct acrosome, a midpiece and a single flagellum surrounded by the flagellar plasma membrane, overview. The enzyme is localized in acrosome, endonuclear canals and implantation fossa
-
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
-
-
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
-
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
-
-
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
-
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda
-
-
brenda
-
brenda
initially present in the sperm acrosomal vesicle of mammalian spermatozoa as the zymogen form, proacrosin, converted to the active form during the acrosome reaction, after which most acrosin molecules are released from the acrosomal vesicle, with a portion remaining associated with the sperm
brenda