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SanT, a bidomain protein, is essential for nikkomycin biosynthesis of Streptomyces ansochromogenes.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Jia L,Tian Y,Tan H

doi

10.1016/j.bbrc.2007.08.114

subject

Has Abstract

pub_date

2007-11-03 00:00:00

pages

1031-6

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)01826-8

journal_volume

362

pub_type

杂志文章

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