Document Detail

A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticola.
MedLine Citation:
PMID:  17382934     Owner:  NLM     Status:  MEDLINE    
An NADH-dependent trans-2-enoyl-CoA reductase (EC1.1.1.36) from the Gram negative spirochete Treponema denticola was identified, expressed and biochemically characterized. The recombinant protein is a monomeric enzyme with a molecular mass of 44 kDa with a specific activity of 43+/-4.8 U/mg (micromol mg(-1)min(-1)) and K(m) value of 2.7 microM for crotonoyl-CoA. This NADH-dependent trans-2-enoyl-CoA reductase represents the first enzymatically characterized member of a prokaryotic protein family involved in a fatty acid synthesis pathway that is distinct from the familiar fatty acid synthase system.
Sara Tucci; William Martin
Related Documents :
3927984 - A unique cardiac cytosolic acyltransferase with preferential selectivity for fatty acid...
8885234 - Importance of glycolipid synthesis for butyric acid-induced sensitization to shiga toxi...
2405844 - Compartmentation of acetyl coa studied by analysis of tricarboxylic acid cycle acids an...
8567624 - Regulation of fatty acid elongation and initiation by acyl-acyl carrier protein in esch...
8725164 - Phytanic acid oxidation: normal activation and transport yet defective alpha-hydroxylat...
17345564 - Application of mixtures of tartaric acid derivatives in resolution via supercritical fl...
Publication Detail:
Type:  Journal Article     Date:  2007-03-15
Journal Detail:
Title:  FEBS letters     Volume:  581     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-04-10     Completed Date:  2007-06-13     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1561-6     Citation Subset:  IM    
Institute of Botany III, Heinrich-Heine University of Duesseldorf, Universitaetsstrasse 1, 40225 Duesseldorf, Germany. <>
Data Bank Information
Bank Name/Acc. No.:
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Amino Acid Sequence
Bacterial Proteins / chemistry*,  genetics,  isolation & purification
Cloning, Molecular
Fatty Acids / biosynthesis
Molecular Sequence Data
Molecular Weight
NADH, NADPH Oxidoreductases / chemistry*,  genetics,  isolation & purification
Oxidoreductases Acting on CH-CH Group Donors
Recombinant Proteins / chemistry*,  genetics,  isolation & purification
Treponema denticola / enzymology*
Reg. No./Substance:
0/Bacterial Proteins; 0/Fatty Acids; 0/Recombinant Proteins; EC 1.3.-/Oxidoreductases Acting on CH-CH Group Donors; EC reductase (NADPH); EC 1.6.-/NADH, NADPH Oxidoreductases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Self-assembly of the isolated KCNQ2 subunit interaction domain.
Next Document:  Plant aquaporins: novel functions and regulation properties.