PMID: 3753434May 1, 1986Paper

Characterization of three-fraction mycobacillin synthetase

The Biochemical Journal
N K MukhopadhyayS K BOSE

Abstract

Mycobacillin synthetase lacks aspartic acid racemase, alanine racemase and glutamic acid racemase activities. The enzyme also does not respond to ATP-[32P]Pi exchange, nor does it catalyse the antibiotic synthesis in presence of amino acids of configuration opposite to that present in the molecule. Preincubation with optical isomers of opposite configuration inhibited the ATP-[32P]Pi exchange reaction to the extent of 60-90%. None of the three fractions of mycobacillin synthetase contained a pantothenic acid arm. Two molecules of ATP are required to synthesize one peptide bond of mycobacillin. Intermediate peptides of mycobacillin are not covalently linked to the three-fraction mycobacillin synthetase.

Citations

Jan 1, 1990·Critical Reviews in Biotechnology·M M Nakano, P Zuber
Feb 20, 2002·Chemical Reviews·Hans von DöhrenRainer Zocher

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