Org Lett. 2009 Oct 15;11(20):4748-51. doi: 10.1021/ol901961q.

Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase.

Source

Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

Abstract

A study of DXP synthase has revealed flexibility in the acceptor substrate binding pocket for nonpolar substrates and has uncovered new details of the catalytic mechanism to show that pyruvate can act as both donor and acceptor substrate.

PMID:: 19778006; [PubMed - indexed for MEDLINE]
PMCID:: PMC2761658

Free PMC Article

Images from this publication.See all images (3)Free text

Publication Types, MeSH Terms, Substances, Grant Support

Publication Types

MeSH Terms

Substances

Grant Support

LinkOut - more resources

Full Text Sources

Supplemental Content

Save items

Click here to read article using PubReader

Related citations in PubMed

Rhodobacter capsulatus 1-deoxy-D-xylulose 5-phosphate synthase: steady-state kinetics and substrate binding. [Biochemistry. 2003]
Rhodobacter capsulatus 1-deoxy-D-xylulose 5-phosphate synthase: steady-state kinetics and substrate binding.
Eubanks LM, Poulter CD. Biochemistry. 2003 Feb 4; 42(4):1140-9.
High-performance liquid chromatography assay for 1-deoxy-D-xylulose 5-phosphate synthase activity using fluorescence detection. [J Chromatogr A. 2003]
High-performance liquid chromatography assay for 1-deoxy-D-xylulose 5-phosphate synthase activity using fluorescence detection.
Han YS, Sabbioni C, van der Heijden R, Verpoorte R. J Chromatogr A. 2003 Feb 7; 986(2):291-6.
Observation of thiamin-bound intermediates and microscopic rate constants for their interconversion on 1-deoxy-D-xylulose 5-phosphate synthase: 600-fold rate acceleration of pyruvate decarboxylation by D-glyceraldehyde-3-phosphate. [J Am Chem Soc. 2012]
Observation of thiamin-bound intermediates and microscopic rate constants for their interconversion on 1-deoxy-D-xylulose 5-phosphate synthase: 600-fold rate acceleration of pyruvate decarboxylation by D-glyceraldehyde-3-phosphate.
Patel H, Nemeria NS, Brammer LA, Freel Meyers CL, Jordan F. J Am Chem Soc. 2012 Nov 7; 134(44):18374-9. Epub 2012 Oct 26.
Tools for discovery of inhibitors of the 1-deoxy-D-xylulose 5-phosphate (DXP) synthase and DXP reductoisomerase: an approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa. [FEMS Microbiol Lett. 2000]
Tools for discovery of inhibitors of the 1-deoxy-D-xylulose 5-phosphate (DXP) synthase and DXP reductoisomerase: an approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa.
Altincicek B, Hintz M, Sanderbrand S, Wiesner J, Beck E, Jomaa H. FEMS Microbiol Lett. 2000 Sep 15; 190(2):329-33.
A mutant pyruvate dehydrogenase E1 subunit allows survival of Escherichia coli strains defective in 1-deoxy-D-xylulose 5-phosphate synthase. [FEBS Lett. 2006]
A mutant pyruvate dehydrogenase E1 subunit allows survival of Escherichia coli strains defective in 1-deoxy-D-xylulose 5-phosphate synthase.
Sauret-Güeto S, Urós EM, Ibáñez E, Boronat A, Rodríguez-Concepción M. FEBS Lett. 2006 Feb 6; 580(3):736-40. Epub 2006 Jan 9.

See reviews... See all...

Cited by 2 PubMed Central articles

Selective inhibition of E. coli 1-deoxy-D-xylulose-5-phosphate synthase by acetylphosphonates(). [Medchemcomm. 2012]
Selective inhibition of E. coli 1-deoxy-D-xylulose-5-phosphate synthase by acetylphosphonates().
Smith JM, Vierling RJ, Meyers CF. Medchemcomm. 2012; 3:65-67. Epub 2011 Oct 26.
1-Deoxy-D-xylulose 5-phosphate synthase catalyzes a novel random sequential mechanism. [J Biol Chem. 2011]
1-Deoxy-D-xylulose 5-phosphate synthase catalyzes a novel random sequential mechanism.
Brammer LA, Smith JM, Wade H, Meyers CF. J Biol Chem. 2011 Oct 21; 286(42):36522-31. Epub 2011 Aug 30.

Related information

Related Citations
Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
Gene
Gene records that cite the current articles. Citations in Gene are added manually by NCBI or imported from outside public resources.
Gene (GeneRIF)
Gene records that have the current articles as Reference into Function citations (GeneRIFs). NLM staff reviewing the literature while indexing MEDLINE add GeneRIFs manually.
Nucleotide (Weighted)
Nucleotide records associated with the current articles through the Gene database. These are the related sequences on the Gene record that are added manually by NCBI.
Protein (RefSeq)
NCBI protein Reference Sequences (RefSeqs) that are cited in the current articles, included in the corresponding Gene Reference into Function, or that include the PubMed articles as references.
Protein (Weighted)
Protein records associated with the current articles through related Gene database records. These are the related sequences on the Gene record that are added manually by NCBI.
Protein Clusters
Clusters of related proteins from the Protein Clusters database that cite the current articles. Sources of references in Protein Clusters include the associated Gene and Conserved Domain records as well as NCBI added citations.
References for this PMC Article
Citation referenced in PubMed article. Only valid for PubMed citations that are also in PMC.
Substance (MeSH Keyword)
PubChem chemical substance (submitted) records that are classified under the same Medical Subject Headings (MeSH) controlled vocabulary as the current articles.
Taxonomy via GenBank
Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).
GEO Profiles
Gene Expression Omnibus (GEO) Profiles of molecular abundance data. The current articles are references on the Gene record associated with the GEO profile.
Free in PMC
Free full text articles in PMC
Cited in PMC
Full-text articles in the PubMed Central Database that cite the current articles.

Recent activity

Clear Turn Off Turn On

Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase.
Revealing substrate promiscuity of 1-deoxy-D-xylulose 5-phosphate synthase.
Org Lett. 2009 Oct 15 ;11(20):4748-51. doi: 10.1021/ol901961q.

PubMed

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

PubMed

Result Filters

Display Settings:

Send to: