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Literature summary for 3.5.1.14 extracted from

  • Kumpe, E.; Löffler, H.G.; Schneider, F.
    Studies on the Zn2+/Co2+ exchange with acylamino acid amidohydrolase from pig kidney (1981), Z. Naturforsch. C, 36, 951-955.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
Sus scrofa
diethyldithiocarbamate
-
Sus scrofa
Tris-(2-amino-ethyl)-amine
-
Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+
-
Sus scrofa
Zn2+ enzyme contains Zn as prosthetic metal Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetyl-L-methionine Sus scrofa
-
L-methionine + acetate
-
?

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
pig
-

Purification (Commentary)

Purification (Comment) Organism
-
Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-DL-methionine + H2O
-
Sus scrofa DL-methionine + acetate
-
?
N-acetyl-L-methionine
-
Sus scrofa L-methionine + acetate
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
up to apoenzyme is less heat sensitive than the active holoenzyme Sus scrofa