Linked Life Data

18068978

Source:http://linkedlifedata.com/resource/pubmed/id/18068978

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2008-5-21
pubmed:abstractText
OxyB catalyzes the first oxidative phenol coupling reaction in vancomycin biosynthesis. OxyB is a P450 hemoprotein whose activity is strictly dependent upon the presence of molecular oxygen. Here, it was shown that label from (18)O(2) is not incorporated into the monocyclic product during catalysis by OxyB. In addition, it was shown that OxyB can convert a model hexapeptide substrate containing (R)-Tyr6, instead of (S)-Tyr6, covalently linked as a C-terminal thioester to a peptidyl carrier protein (PCP-7S) derived from the vancomycin non-ribosomal peptide synthetase (NRPS), into the corresponding epimeric monocyclic product. The binding of this epimeric hexapeptide-PCP conjugate to the Fe(III) form of OxyB, as monitored by UV-vis spectroscopy, revealed a K(d)=35+/-5 microM. Thus, the enzyme reveals a surprising lack of stereospecificity in the binding and transformation of these epimeric substrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1464-3405
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3081-4
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
New insights into the first oxidative phenol coupling reaction during vancomycin biosynthesis.
pubmed:affiliation
Department of Chemistry, Institute of Organic Chemistry, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't