Issue 18, 2001

Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibioticsElectronic supplementary information (ESI) available: SDS-PAGE analysis of HmO and molecular weight analysis of HmO protein by ESI-MS and GC/CI-MS of the enzymatic conversion of 3,5DHMA with HmO. See http://www.rsc.org/suppdata/cc/b1/b103548g/

Abstract

ORF22 from the chloroeremomycin gene cluster has been cloned, expressed and characterised as a hydroxymandelate oxidase (HmO) that is involved in the formation of both (S)-4-hydroxyphenylglycine and (S)-3,5-dihydroxyphenylglycine.

Supplementary files

Article information

Article type
Communication
Submitted
19 Apr 2001
Accepted
24 Jul 2001
First published
28 Aug 2001

Chem. Commun., 2001, 1752-1753

Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibiotics

T. Li, O. W. Choroba, E. H. Charles, A. M. Sandercock, D. H. Williams and J. B. Spencer, Chem. Commun., 2001, 1752 DOI: 10.1039/B103548G

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