An active site mutant of Escherichia coli cyclopropane fatty acid synthase forms new non-natural fatty acids providing insights on the mechanism of the enzymatic reaction.

E, Guangqi; Drujon, Thierry; Correia, Isabelle; Ploux, Olivier; Guianvarc'h, Dominique

E, Guangqi; Drujon, Thierry; Correia, Isabelle; Ploux, Olivier; Guianvarc'h, Dominique.

Affiliation

E G; UPMC Univ Paris 06, UMR 7203, Laboratoire des BioMolécules, 4, place Jussieu, F-75005 Paris, France; Chimie ParisTech ENSCP, Laboratoire Charles Friedel, 11 rue Pierre et Marie Curie, 75231 Paris Cedex 05, France.

Biochimie ; 95(12): 2336-44, 2013 Dec.

Article in En | MEDLINE | ID: mdl-23954860

Subject(s)

Fatty Acids/biosynthesis; Methyltransferases/genetics; Methyltransferases/metabolism; Amino Acid Substitution; Catalytic Domain; Escherichia coli/enzymology; Esters/chemistry; Fatty Acids/chemistry; Nuclear Magnetic Resonance, Biomolecular

Key words

AdoHcy; AdoMet; CFAS; CMAS; CS; Cyclopropane fatty acid synthase; DMDS; DMSO; EI; Enzyme mechanism; FAME; Fatty acid methyl ester; GC; GC/MS; IPTG; Mycolic acid methyltransferase; S-adenosyl-l-homocysteine; S-adenosyl-l-methionine; cyclopropane fatty acid synthase; cyclopropane mycolic acid synthase; cyclopropane synthase; dimethyl disulfide; dimethylsulfoxide; electron impact; fatty acid methyl ester; gas chromatography; gas chromatography coupled to mass spectrometry; isopropyl ß-d-1-thiogalactopyranoside

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Fatty Acids / Methyltransferases Language: En Journal: Biochimie Year: 2013 Type: Article Affiliation country: France

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