| Literature DB >> 4462556 |
M Nakatani, M Morimoto, T Noguchi, R Kido.
Abstract
Kynurenine transaminase activity in rat liver was found in both the mitochondrial and supernatant fractions. The mitochondrial and supernatant fractions contained (a) kynurenine-pyruvate transaminase, which showed a preference for pyruvate as amino acceptor and a pH optimum between 8.0 and 8.5, and (b) kynurenine-alpha-oxoglutarate transaminase, with a preference for alpha-oxoglutarate and a pH optimum between 6.0 and 6.5. Possible roles of these enzymes in tryptophan metabolism in the liver are discussed.Entities:
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Year: 1974 PMID: 4462556 PMCID: PMC1168385 DOI: 10.1042/bj1430303
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857