Escherichia coli cytosolic glycerophosphodiester phosphodiesterase (UgpQ) requires Mg2+, Co2+, or Mn2+ for its enzyme activity.
J Bacteriol
; 190(4): 1219-23, 2008 Feb.
Article
em En
| MEDLINE
| ID: mdl-18083802
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Diester Fosfórico Hidrolases
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Proteínas de Escherichia coli
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Escherichia coli
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Metais
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article