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Data on Bioscience and Bioengineering Reported by Researchers at Nagoya University (Phospholipase D as a catalyst: application in phospholipid...

August 26, 2014



Data on Bioscience and Bioengineering Reported by Researchers at Nagoya University (Phospholipase D as a catalyst: application in phospholipid synthesis, molecular structure and protein engineering)

By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Life Science Research have been presented. According to news reporting originating in Nagoya, Japan, by NewsRx journalists, research stated, "Phospholipase D (PLD) is a useful enzyme for its transphosphatidylation activity, which enables the enzymatic synthesis of various phospholipids (PLs). Many reports exist on PLD-mediated synthesis of natural and tailor-made PLs with functional head groups, from easily available lecithin or phosphatidylcholine."

The news reporters obtained a quote from the research from Nagoya University, "Early studies on PLD-mediated synthesis mainly employed enzymes of plant origin, which were later supplanted by ones from microorganisms, especially actinomycetes. Many PLDs are members of the PLD superfamily, having one or two copies of a signature sequence, HxKxxxxD or HKD motif, in the primary structures. PLD superfamily members share a common core structure, and thereby, a common catalytic mechanism. The catalysis proceeds via two-step reaction with the formation of phosphatidyl-enzyme intermediate. Both of the two catalytic His residues are critical in the reaction course, where one acts as a nucleophile, while the other functions as a general acid/base. PLD is being engineered to improve its activity and stability, alter head group specificity and further identify catalytically important residues. Since the knowledge on PLD enzymology is constantly expanding, this review focuses on recent advances in the field, regarding PLD-catalyzed synthesis of bioactive PLs, deeper understanding of substrate recognition and binding mechanism, altering substrate specificity, and improving thermostability."

According to the news reporters, the research concluded: "We introduced some of our recent results in combination with existing facts to further deepen the story on the nature of this useful enzyme."

For more information on this research see: Phospholipase D as a catalyst: application in phospholipid synthesis, molecular structure and protein engineering. Journal of Bioscience and Bioengineering, 2013;116(3):271-80. (Elsevier - www.elsevier.com; Journal of Bioscience and Bioengineering - www.elsevier.com/wps/product/cws_home/505516)

Our news correspondents report that additional information may be obtained by contacting J. Damnjanovi?, Laboratory of Molecular Biotechnology, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8601, Japan (see also Life Science Research).

Keywords for this news article include: Asia, Japan, Nagoya, Engineering, Life Science Research.

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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