Publication:Life Science Weekly
Date:Tuesday April 23rd, 2013
Page:1302
Summary
…Quote from the research from Carleton University, “Although CGS and TS have been characterized in the model
organisms Escherichia coli and Arabidopsis thaliana, little information is available on these enzymes in other, particularly
plant, species.
Text
2013 APR 23 (NewsRx) — By a News Reporter-Staff News Editor at Life Science Weekly — Investigators discuss new
findings in Sulfur Amino Acids. According to news reporting out of Ottawa, Canada, by NewsRx editors, research stated, “In
plants, cystathionine ?-synthase (CGS) and threonine synthase (TS) compete for the branch-point metabolite O-phosphol-
homoserine. These enzymes are potential targets for metabolic engineering studies, aiming to alter the flux through the
competing methionine and threonine biosynthetic pathways, with the goal of increasing methionine production.”
Our news journalists obtained a quote from the research from Carleton University, “Although CGS and TS have been
characterized in the model organisms Escherichia coli and Arabidopsis thaliana, little information is available on these
enzymes in other, particularly plant, species. The functional CGS and TS coding sequences from the grain legumes Cicer
arietinum (chickpea) and Lens culinaris (lentil) identified in this study share approximately 80% amino acid sequence identity
with the corresponding sequences from Glycine max. At least 7 active-site residues of grain legume CGS and TS are
conserved in the model bacterial enzymes, including the catalytic base.”
According to the news editors, the research concluded: “Putative processing sites that remove the targeting sequence
and result in functional TS were identified in the target species.”
For more information on this research see: Identification of cystathionine ?-synthase and threonine synthase from Cicer
arietinum and Lens culinaris. Biochemistry and Cell Biology, 2013;91(2):95-101. Biochemistry and Cell Biology can be
contacted at: National Research Council of Canada, NRC Communications & Corporate Relations, 1200 Montreal Road,
Bldg. M-58, Ottawa, Ontario, Canada K1A 0R6. (NRC Research Press – www.nrcresearchpress.com/; Biochemistry and
Cell Biology – www.nrcresearchpress.com/journal/bcb)
Our news journalists report that additional information may be obtained by contacting D.J. Morneau, Dept. of Biology,
Carleton University, Ottawa, ON K1S 5B6, Canada.
Publisher contact information for the journal Biochemistry and Cell Biology is: National Research Council of Canada,
NRC Communications & Corporate Relations, 1200 Montreal Road, Bldg. M-58, Ottawa, Ontario, Canada K1A 0R6.
Keywords for this news article include: Ottawa, Canada, Ontario, Synthase, Cystathionine, Sulfur Amino Acids, Diamino
Amino Acids, Enzymes and Coenzymes, Dicarboxylic Amino Acids, North and Central America.
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