By a News Reporter-Staff News Editor at Biotech Week -- Fresh data on Mycobacterium Infections are presented in a new report. According to news reporting originating in San Francisco, California, by NewsRx journalists, research stated, "The characterization of functionally diverse enzyme superfamilies provides the opportunity to identify evolutionarily conserved catalytic strategies, as well as amino acid substitutions responsible for the evolution of new functions or specificities. Isopropylmalate synthase (IPMS) belongs to the DRE-TIM metallolyase superfamily."
The news reporters obtained a quote from the research from the University of California, "Members of this superfamily share common active site elements, including a conserved active site helix and an HXH divalent metal binding motif, associated with stabilization of a common enolate anion intermediate. These common elements are overlaid by variations in active site architecture resulting in the evolution of a diverse set of reactions that include condensation, lyase/aldolase, and carboxyl transfer activities. Here, using IPMS, an integrated biochemical and bioinformatics approach has been utilized to investigate the catalytic role of residues on an active site helix that is conserved across the superfamily. The construction of a sequence similarity network for the DRE-TIM metallolyase superfamily allows for the biochemical results obtained with IPMS variants to be compared across superfamily members and within other condensation-catalyzing enzymes related to IPMS. A comparison of our results with previous biochemical data indicates an active site arginine residue (R80 in IPMS) is strictly required for activity across the superfamily, suggesting that it plays a key role in catalysis, most likely through enolate stabilization."
According to the news reporters, the research concluded: "In contrast, differential results obtained from substitution of the C-terminal residue of the helix (Q84 in IPMS) suggest that this residue plays a role in reaction specificity within the superfamily."
For more information on this research see: Mechanistic and Bioinformatic Investigation of a Conserved Active Site Helix in alpha-Isopropylmalate Synthase from Mycobacterium tuberculosis, a Member of the DRE-TIM Metallolyase Superfarnily. Biochemistry, 2014;53(18):2915-2925. Biochemistry can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Biochemistry - www.pubs.acs.org/journal/bichaw)
Our news correspondents report that additional information may be obtained by contacting A.K. Casey, University of California, Calif Inst Quantitat Biosci, San Francisco, CA 94158, United States. Additional authors for this research include M.A. Hicks, J.L. Johnson, P.C. Babbitt and P.A. Frantom (see also Mycobacterium Infections).
Keywords for this news article include: Biotechnology, Synthase, California, Biochemical, Biochemistry, San Francisco, United States, Actinobacteria, Bioengineering, Mycobacteriaceae, Gram-Positive Rods, Enzymes and Coenzymes, Applied Bioinformatics, Gram-Positive Bacteria, Mycobacterium Infections, North and Central America, Actinomycetales Infections
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