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Literature summary for 3.4.19.1 extracted from

  • Mitta, M.; Miyagi, M.; Kato, I.; Tsunasawa, S.
    Identification of the catalytic triad residues of porcine liver acylamino acid-releasing enzyme (1998), J. Biochem., 123, 924-931.
    View publication on PubMed
Search for more literature for 3.4.19.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli Sus scrofa

Protein Variants

Protein Variants Comment Organism
A587S no hydrolytic activity Sus scrofa
N675S no hydrolytic activity Sus scrofa
Y707H no hydrolytic activity Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.49
-
 N-acetyl-Met-Ala wild-type enzyme Sus scrofa
0.56
-
 N-acetyl-Met-Ala recombinant wild-type enzyme Sus scrofa
0.68
-
 N-acetyl-Met-Ala mutant enzyme D562N Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-Met-Ala + H2O
-
 Sus scrofa N-acetyl-Met + Ala
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
13.4
-
 N-acetyl-Met-Ala mutant enzyme D562N Sus scrofa
29
-
 N-acetyl-Met-Ala recombinant wild-type enzyme Sus scrofa
33
-
 N-acetyl-Met-Ala wild-type enzyme Sus scrofa