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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
4.3.1.3 Cys273A mutant yields rectangular crystals Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.3 53559
-
4 * 53559, calculation from sequence of amino acid 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 additional information Pseudomonas putida
-
?
-
?

Organism

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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