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Literature summary 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

EC Number Inhibitors Comment Organism Structure
3.5.1.14 1,10-phenanthroline
-
 Sus scrofa
3.5.1.14 diethyldithiocarbamate
-
 Sus scrofa
3.5.1.14 Tris-(2-amino-ethyl)-amine
-
 Sus scrofa

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.14 Sus scrofa
-
 pig
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.14
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.14 kidney
-
 Sus scrofa
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.14 45
-
 up to apoenzyme is less heat sensitive than the active holoenzyme Sus scrofa