Issue 5, 1994

Mechanism of dethiobiotin synthetase—characterisation of the 8-aminocarbamate of (7R,8S)-7,8 diaminononanoate as an enzyme-bound intermediate

Abstract

Enzymatically catalysed formation of the ureido ring of dethiobiotin 2 from (7R, 8S)-7,8-diaminononanoate 3 by purified E. coli dethiobiotin synthetase involves the formal hydrolysis of one equivalent of ATP, a combination of substrate loading and trapping experiments show that the carbamate 5 is an intermediate in the synthesis of dethiobiotin from 3.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1994, 559-560

Mechanism of dethiobiotin synthetase—characterisation of the 8-aminocarbamate of (7R,8S)-7,8 diaminononanoate as an enzyme-bound intermediate

R. L. Baxter, A. J. Ramsey, L. A. Mclver and H. C. Baxter, J. Chem. Soc., Chem. Commun., 1994, 559 DOI: 10.1039/C39940000559

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