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. 1986 Nov 15;240(1):265–268. doi: 10.1042/bj2400265

Role of ATP and enzyme-bound nascent peptides in the control of elongation for mycobacillin synthesis.

S K Ghosh, S Majumder, N K Mukhopadhyay, S K Bose
PMCID: PMC1147403  PMID: 3103608

Abstract

The enzyme fraction A, a constituent of the three-fraction (A, B and C) enzyme complex mycobacillin synthetase, elongated tri- and tetra-peptides, under enzyme-bound conditions, to tetra- and penta-peptides respectively in the presence of the 'next' amino acid (in the mycobacillin sequence). The enzyme fraction B synthesized hexapeptide from free pentapeptide and the next amino acid, but synthesized heptapeptide from hexapeptide only under enzyme-bound conditions in the presence of the next amino acid. Similarly, the enzyme fraction C synthesized decapeptide from free nonapeptide in the presence of the next amino acid, but undecapeptide only from enzyme-bound decapeptide in the presence of the next amino acid during the elongation process. The Km values for the initiating reactions for each of the three enzyme fractions were 6-7-fold lower than those for the succeeding reactions catalysed by each of the enzyme fractions. The specificity of the initiation and elongation is discussed in the light of these findings.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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