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Literature summary for 3.4.19.1 extracted from

  • Chongcharoen, K.; Sharma, K.K.
    Characterization of trypsin: modified bovine lens acylpeptide hydrolase (1998), Biochem. Biophys. Res. Commun., 247, 136-141.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
lens
-
Bos taurus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1490
-
-
Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formylmethionine p-nitroanilide + H2O
-
Bos taurus formylmethionine + p-nitroaniline
-
?
additional information the trypsin-modified enzyme is able to unblock alphaA-crystallin and displays endoprotease activity unlike the native enzyme Bos taurus ?
-
?
N-acetyl-Ala p-nitroanilide + H2O
-
Bos taurus N-acetyl-Ala + p-nitroaniline
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8 hydrolysis of N-acetyl-Ala p-nitroanilide Bos taurus