This Article Full Text Full Text (PDF) Other Versions of this Article: JB.01223-07v1 190/4/1219    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Google Scholar Articles by Ohshima, N. Articles by Takio, K. PubMed PubMed Citation Articles by Ohshima, N. Articles by Takio, K.

Escherichia coli Cytosolic Glycerophosphodiester Phosphodiesterase (UgpQ) Requires Mg²⁺, Co²⁺, or Mn²⁺ for Its Enzyme Activity

RIKEN SPring-8 Center, Harima Institute, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan

Received 30 July 2007/ Accepted 30 November 2007

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. These results clarify how E. coli utilizes glycerophosphodiesters using two homologous enzymes, UgpQ and GlpQ.

Published ahead of print on 14 December 2007.