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Literature summary for 5.1.1.10 extracted from

  • Lim, Y.H.; Yoshimura, T.; Kurokawa, Y.; Esaki, N.; Soda, K.
    Nonstereospecific transamination catalyzed by pyridoxal phosphate-dependent amino acid racemases of broad substrate specificity (1988), J. Biol. Chem., 273, 4001-4005.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
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-
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Reaction

Reaction Comment Organism Reaction ID
an L-amino acid = a D-amino acid enzyme abstracts a hydrogen nonstereospecifically from C-4' of the coenzyme Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + L-ornithine
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Pseudomonas putida D-glutamate + L-glutamate
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?
additional information catalyzes nonstereospecific transamination: production of D-Glu and L-Glu from 2-oxoglutarate through transamination with L-Orn Pseudomonas putida ?
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?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate pyridoxal phosphate enzyme Pseudomonas putida
pyridoxal 5'-phosphate dependent on Pseudomonas putida