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Literature summary for 2.6.1.38 extracted from

  • Roos, U.; Mattern, S.; Schrempf, H.; Bormann, C.
    Histidine aminotransferase activity in Streptomyces tendae and its correlation with nikkomycin production (1992), FEMS Microbiol. Lett., 97, 185-190.
No PubMed abstract available
Search for more literature for 2.6.1.38

Inhibitors

Inhibitors Comment Organism Structure
Bromopyruvate
-
 Streptomyces tendae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
 gel filtration Streptomyces tendae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
imidazol-5-yl-pyruvate + L-glutamate Streptomyces tendae involved in nikkomycin biosynthesis, essential in the utilization of imidazol-L-lactate and imidazole pyruvate as carbon sources histidine + 2-oxoglutarate
-
 r

Organism

Organism UniProt Comment Textmining
Streptomyces tendae
-
 Tue901/AEC6, mutant hut-11
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0015
-
 substrate L-tryptophan Streptomyces tendae
0.0019
-
 substrate L-histidine Streptomyces tendae
0.002
-
 substrate L-tyrosine Streptomyces tendae
0.0021
-
 substrate L-phenylalanine Streptomyces tendae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
imidazol-5-yl-pyruvate + L-glutamate
-
 Streptomyces tendae L-histidine + 2-oxoglutarate
-
 r
imidazol-5-yl-pyruvate + L-glutamate involved in nikkomycin biosynthesis, essential in the utilization of imidazol-L-lactate and imidazole pyruvate as carbon sources Streptomyces tendae histidine + 2-oxoglutarate
-
 r

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50 70 preincubation of the reaction mixture at 50, 60 and 70°C results in a increase of the reaction rate Streptomyces tendae

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate activity is dependent on the coenzyme and a keto acceptor such as pyruvate or 2-oxoglutarate Streptomyces tendae