| Literature DB >> 18266 |
G J Murray, G E Clark, M A Parniak, T Viswanatha.
Abstract
The conversion of L-lysine to its corresponding epsilon-N-hydroxy derivative has been achieved for the first time by cell-free extracts of Aerobacter aerogenes 62-1. Partial fractionation by differential centrifugation (at 12 000 X g) revealed that both supernatant and pellet are essential for maximum enzymatic activity. The omega-N-hydroxylase (EC 1.14.99) was found to function optimally at pH 7-7.5 and exhibited an apparent Km of about 75 muM for L-lysine. L(+)-Lactate or DL-lactate and pyruvate greatly stimulate the omega-N-hydroxylase activity. The system is strongly inhibited by arsenite and sulfite.Entities:
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Year: 1977 PMID: 18266 DOI: 10.1139/o77-090
Source DB: PubMed Journal: Can J Biochem ISSN: 0008-4018