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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).