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B6db references: 17825260

type Journal Article
authors Jia L, Tian Y, Tan H
title SanT, a bidomain protein, is essential for nikkomycin biosynthesis of Streptomyces ansochromogenes
journal Biochem Biophys Res Commun
Activity sant
Family sant
sel selected
ui 17825260
year (2007)
volume 362
number 4
pages 1031-6
abstract Nikkomycins act as a competitive inhibitor of chitin synthetase and display potent activities against phytopathogenic and human pathogenic fungi. sanT is located in the gene cluster of nikkomycin biosynthesis in Streptomyces ansochromogenes. Sequence analysis revealed that the deduced product of sanT has an unusual domain structure, which consists of an N-terminal acyl carrier protein (ACP) domain and a C-terminal aminotransferase (AMT) domain. Gene disruption and complementation indicated that sanT is essential for nikkomycin biosynthesis. Each domain of SanT was overexpressed in Escherichia coli and then purified. ACP domain is posttranslationally modified with phosphopantetheine (Ppant) prosthetic group at Ser-33. AMT domain catalyzes the transamination of 4-pyridyl-2-oxo-4-hydroxyisovalerate (POHIV), a precursor of peptidyl moiety of nikkomycins, to pyridylhomothreonine (PHT) in vitro. The two domains function independently but both are essential for nikkomycin biosynthesis. The biochemical and genetic evidences suggested that SanT is possibly a bifunctional protein, participating in the biosynthesis of peptidyl moiety and the assembly of nikkomycins.
last changed 2019/06/20 13:18

B6db references