Cyclopropane fatty acid synthase from Oenococcus oeni: expression in Lactococcus lactis subsp. cremoris and biochemical characterization View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-11

AUTHORS

Thi Mai Huong To, Cosette Grandvalet, Hervé Alexandre, Raphaëlle Tourdot-Maréchal

ABSTRACT

Bacterial cyclopropane fatty acid synthases (CFA synthases) catalyze the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the double bond of a lipid chain, thereby forming a cyclopropane ring. CFAs contribute to resistance to acidity, dryness, and osmotic imbalance in many bacteria. This work describes the first biochemical characterization of a lactic acid bacterium CFA synthase. We have overexpressed Oenococcus oeni CFA synthase in E. coli in order to purify the enzyme. The optimum cyclopropanation activity was obtained at pH 5.6 and 35.8 °C. The high K(m) (AdoMet) value obtained (2.26 mM) demonstrates the low affinity of O. oeni enzyme toward the L. lactis subsp. cremoris unsaturated phospholipids. These results explain the partial complementation of the L. lactis subsp. cremoris cfa mutant by the O. oeni cfa gene and suggest a probable substrate specificity of the O. oeni enzyme. The current study reveals an essential hypothesis about the specificity of O. oeni CFA synthase which could play a key function in the acid tolerance mechanisms of this enological bacterium. More... »

PAGES

1063-1074

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00203-015-1143-y

DOI

http://dx.doi.org/10.1007/s00203-015-1143-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1032266962

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26294376


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