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Literature summary extracted from

  • Galpin, J.D.; Ellis, B.E.; Tanner, M.E.
    The Inactivation of Histidine Ammonia-Lyase by L-Cysteine and Oxygen: Modification of the Electrophilic Center (1999), J. Am. Chem. Soc., 121, 10840-10841.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.1.3 expression in Escherichia coli Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.3.1.3 L-cysteine 50 mM, complete inaction at basic pH in the presence of O2 is due to a covalent modification of the enzyme Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.1.3 L-histidine Pseudomonas putida
-
urocanate + NH3
-
r

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.3 Pseudomonas putida
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.3 recombinant histidase Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.3 L-histidine
-
Pseudomonas putida urocanate + NH3
-
r

Synonyms

EC Number Synonyms Comment Organism
4.3.1.3 HAL
-
Pseudomonas putida