Mechanistic and stereochemical studies of glycine oxidase from Bacillus subtilis strain R5.

Abstract

Glycine oxidase gene from a strain of Bacillus subtilis was cloned and expressed in Escherichia coli. The purified enzyme was found, by mass spectrometry, to have a protein M(r) of 40763 (value of 40761.6 predicted from DNA sequence) and a FAD prosthetic group M(r) of 785.1 (theoretical value of 785.5). Glycine oxidase optimally catalyzes the conversion of… (More)
DOI: 10.1021/bi100553n

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