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Reports on Lactobacillus Findings from Kwangwoon University Provide New Insights (Crystal structure and thermodynamic properties of D-lactate...

August 5, 2014



Reports on Lactobacillus Findings from Kwangwoon University Provide New Insights (Crystal structure and thermodynamic properties of D-lactate dehydrogenase from Lactobacillus jensenii)

By a News Reporter-Staff News Editor at Life Science Weekly -- A new study on Gram-Positive Bacteria is now available. According to news reporting from Seoul, South Korea, by NewsRx journalists, research stated, "The thermostable D-lactate dehydrogenase from Lactobacillus jensenii (LjD-LDH) is a key enzyme in the production of the D-form of lactic acid from pyruvate concomitant with the oxidation of NADH to NAD+. The polymers of ID-lactic acid are used as biodegradable bioplastics."

The news correspondents obtained a quote from the research from Kwangwoon University, "The crystal structures of LjD-LDH and in complex with NADI(+) were determined at 2.13 and 2.60 angstrom resolutions, respectively. The LjD-LDH monomer consists of the N-terminal substrate-binding domain and the C-terminal NAD-binding domain. The LjD-LDH forms a homodimeric structure, and the C-terminal NAD-binding domain mostly enables the dimerization of the enzyme. The NAD cofactor is bound to the GxGxxG NAD-binding motif located between the two domains. Structural comparisons of LjD-LDH with other D-LDHs reveal that LjD-LDH has unique amino acid residues at the linker region, which indicates that the open-close dynamics of LjD-LDH might be different from that of other D-LDHs. Moreover, thermostability experiments showed that the T-50(10) value of LjD-LDH (54.5 degrees C) was much higher than the commercially available D-lactate dehydrogenase (42.7 degrees C)."

According to the news reporters, the research concluded: "In addition, LjD-LDH has at least a 7 degrees C higher denaturation temperature compared to commercially available D-LDHs."

For more information on this research see: Crystal structure and thermodynamic properties of D-lactate dehydrogenase from Lactobacillus jensenii. International Journal of Biological Macromolecules, 2014;68():151-157. International Journal of Biological Macromolecules can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands. (Elsevier - www.elsevier.com; International Journal of Biological Macromolecules - www.elsevier.com/wps/product/cws_home/525446)

Our news journalists report that additional information may be obtained by contacting S. Kim, Kwangwoon Univ, Dept. of Chem Engn, Seoul 139701, South Korea. Additional authors for this research include S.A. Gu, Y.H. Kim and K.J. Kim (see also Gram-Positive Bacteria).

Keywords for this news article include: NAD, Asia, Seoul, South Korea, Lactobacillus, Lactobacillales, Lactobacillaceae, Gram-Positive Rods, Enzymes and Coenzymes, Gram-Positive Bacteria, Lactate Dehydrogenases, Alcohol Oxidoreductases, Gram-Positive Asporogenous Rods

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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