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

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.

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Bibliographic Details
Published inChemical communications (Cambridge, England) no. 18; pp. 1752 - 1753
Main Authors Li, T L, Choroba, O W, Charles, E H, Sandercock, A M, Williams, D H, Spencer, J B
Format Journal Article
LanguageEnglish
Published England 21.09.2001
Subjects
Alcohol Oxidoreductases - genetics
Alcohol Oxidoreductases - isolation & purification
Alcohol Oxidoreductases - metabolism
Amino Acids - biosynthesis
Bacterial Proteins
Chromatography, Gas
Gene Expression Regulation, Bacterial
Glycine - analogs & derivatives
Glycine - biosynthesis
Membrane Proteins - genetics
Membrane Proteins - isolation & purification
Membrane Proteins - metabolism
Molecular Structure
Oxidoreductases - genetics
Oxidoreductases - isolation & purification
Oxidoreductases - metabolism
Resorcinols
Spectrophotometry
Vancomycin - analogs & derivatives
Vancomycin - chemistry
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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1359-7345
1364-548X
DOI:10.1039/b103548g