Enzyme Research

Study data from RIKEN update understanding of enzyme research

Published in Lab Business Week, May 11th, 2008

According to a study from Mikazuki, Japan, "Escherichia coli cytosolic glycerophosphodiester phosphodiesterase, UgpQ, functions in the absence of other proteins encoded by the ugp operon and requires Mg2+, Mn2+, or Co2+, in contrast to Ca2+-dependent periplasmic glycerophosphodiester phosphodiesterase, GlpQ."

"UgpQ has broad substrate specificity toward various glycerophosphodiesters, producing sn-glycerol-3-phosphate and the corresponding alcohols. UgpQ accumulates under conditions of phosphate starvation, suggesting that it allows the utilization of glycerophosphodiesters as a source of phosphate," wrote N. Ohshima and colleagues, RIKEN.

The...

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Source: Lab Business Week (2008-05-11)

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