Literature summary for 4.3.1.3 extracted from

Schwede, T.F.; Baedeker, M.; Langer, M.; Retey, J.; Schulz, G.E.
Homogenization and crystallization of histidine ammonia-lyase by exchange of a surface cysteine residue (1999), Protein Eng., 12, 151-153.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type and mutant	Pseudomonas putida

Protein Variants

Protein Variants	Comment	Organism
Cys273A	mutant yields rectangular crystals	Pseudomonas putida

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
53559	-	4 * 53559, calculation from sequence of amino acid	Pseudomonas putida

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Pseudomonas putida	-	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Pseudomonas putida

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-histidine	natural substrate	Pseudomonas putida	urocanate + NH3	-	r
additional information	-	Pseudomonas putida	?	-	?

Subunits

Subunits	Comment	Organism
tetramer	4 * 53559, calculation from sequence of amino acid	Pseudomonas putida

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Release 2023.1 (January 2023)