Characterization of the Enzyme BtrD from  Bacillus circulans  and Revision of Its Functional Assignment in the Biosynthesis of Butirosin | Zendy

Truman Andrew W. | Zendy; Huang Fanglu | Zendy; Llewellyn Nicholas M. | Zendy; Spencer Jonathan B. | Zendy

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Characterization of the Enzyme BtrD from Bacillus circulans and Revision of Its Functional Assignment in the Biosynthesis of Butirosin

Author(s) -

Truman Andrew W.,

Huang Fanglu,

Llewellyn Nicholas M.,

Spencer Jonathan B.

Publication year - 2007

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200604194

Subject(s) - moiety , chemistry , biosynthesis , biochemistry , enzyme , stereochemistry , gene cluster , glycosyltransferase , uridine , computational biology , gene , rna , biology

A functional reassignment : BtrD, a protein encoded in the butirosin gene cluster, functions as a deacetylase rather than a nucleotidyltransferase as previously reported. BtrD was found to selectively catalyze the conversion of 2′‐ N ‐acetylparomamine to paromamine, strongly suggesting that butirosin's neosamine moiety originates from uridine diphospho(UDP)‐ N ‐acetylglucosamine (see picture).

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