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Article

Histidine residues 102 and 117 of MelC1 play different roles in the chaperone function for Streptomyces apotyrosinase.

Biochemical and biophysical research communications - 14 Sept 1995

Liaw L L, Lee Y H

Abstract excerpt

MelC1 regulates the copper incorporation and secretion of Streptomyces apotyrosinase (MelC2) via a transient, competent complex formation. His-102 and His-117 of the chaperone-like MelC1 are known to play important roles in this trans-activation activity of MelC1. In this study, we studied the side chain requirement at these two residues for MelC1 function. Substitution of His-117 with polar, charged, or...

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Identifiers

PMID: 7677750
DOI: 10.1006/bbrc.1995.2307

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