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PMID: 19668852 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Prenyltransferase substrate binding pocket flexibility and its application in isoprenoid profiling.

Molecular bioSystems ·Vol. 5 ·No. 9 ·2009-09-00 ·Pages 913-7

Xiao Y, Machacek M, Lee K, Kuzuyama T, Liu P

Abstract

This communication explores prenyltransferase substrate binding pocket flexibility to tag and enrich isoprenoids using affinity-based purification for metabolomic studies.

MeSH Terms

Bacterial Proteins/metabolism Binding Sites Dimethylallyltranstransferase/chemistry,metabolism Diphosphates/metabolism Diterpenes/metabolism Kinetics Metabolomics/methods Naphthoquinones/metabolism Pliability Prenylation Protein Binding Reproducibility of Results Streptomyces/enzymology Terpenes/metabolism

Chemicals

Bacterial Proteins Diphosphates Diterpenes Naphthoquinones Terpenes geranyl diphosphate naphterpin B Dimethylallyltranstransferase

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Xiao Youli

Department of Chemistry, Boston University, MA 02215, USA.

Machacek Miranda

Lee Kent

Kuzuyama Tomohisha

Liu Pinghua

Article Info

Journal

Molecular bioSystems

Abbr.

Mol Biosyst

ISSN

1742-2051

DOI

10.1039/b902370d

Published

2009-09-00

Epub

2009-00-26

Pages

913-7

Language

English

Region

England

NLM ID

101251620

Subset

External Links

PubMed source DOI: 10.1039/b902370d

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Prenyltransferase substrate binding pocket flexibility and its application in isoprenoid profiling.

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