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Literature summary for 3.4.19.1 extracted from

  • Sharma, K.K.; Orthwerth, B.J.
    Bovine lens acylpeptide hydrolase. Purification and characterization of a tetrameric enzyme resistant to urea denaturation and proteolytic inactivation (1993), Eur. J. Biochem., 216, 631-637.
    View publication on PubMed

General Stability

General Stability Organism
fully resistant to digestion by trypsin, chymotrypsin and elastase Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
ampicillin partial Bos taurus
DFP
-
Bos taurus
guanidine/HCl 1 M, complete inactivation Bos taurus
N-acetyl-Ala
-
Bos taurus
N-acetyl-Met
-
Bos taurus
N-acetyl-Val
-
Bos taurus
NEM
-
Bos taurus
penicillin G partial Bos taurus
phenylmethylsulfonyl fluoride
-
Bos taurus
Urea
-
Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
75000
-
4 * 75000, SDS-PAGE Bos taurus
300000
-
gel filtration Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
lens
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-Ala p-nitroanilide + H2O
-
Bos taurus N-acetyl-Ala + p-nitroaniline
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 75000, SDS-PAGE Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Bos taurus