Publications

• Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon.

  Larson T.J., Ehrmann M., Boos W.

  The promoter-proximal gene (glpT) of the glpT-glpQ operon of Escherichia coli encodes a membrane permease responsible for active transport of sn-glycerol 3-phosphate. Promoter-distal glpQ encodes a periplasmic protein which is not required for active transport of sn-glycerol 3-phosphate (Larson, T ... >> More

  The promoter-proximal gene (glpT) of the glpT-glpQ operon of Escherichia coli encodes a membrane permease responsible for active transport of sn-glycerol 3-phosphate. Promoter-distal glpQ encodes a periplasmic protein which is not required for active transport of sn-glycerol 3-phosphate (Larson, T.J., Schumacher, G., and Boos, W. (1982) J. Bacteriol. 152, 1008-1021). This periplasmic protein has now been identified as a phosphodiesterase which hydrolyzes glycerophosphodiesters into sn-glycerol 3-phosphate plus alcohol. The enzyme exhibited broad substrate specificity with respect to the alcohol moiety; sn-glycerol 3-phosphate was released from glycerophosphoethanolamine, glycerophosphocholine, glycerophosphoglycerol, and bis(glycerophospho)glycerol. The enzyme was specific for glycerophosphodiesters; bis(p-nitrophenyl)phosphate, a substrate for other phosphodiesterases, was not hydrolyzed. In a coupled spectrophotometric assay utilizing sn-glycerol 3-phosphate dehydrogenase and NAD, apparent activity was optimal at pH 9 and was stimulated by Ca2+. The substrates of the phosphodiesterase had no affinity for the glpT-encoded active transport system. Thus, the glpQ gene product expands the catabolic capability of the glp regulon to include a variety of glycerophosphodiesters. << Less

  J Biol Chem 258:5428-5432(1983) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Characterization of the Arabidopsis glycerophosphodiester phosphodiesterase (GDPD) family reveals a role of the plastid-localized AtGDPD1 in maintaining cellular phosphate homeostasis under phosphate starvation.

  Cheng Y., Zhou W., El Sheery N.I., Peters C., Li M., Wang X., Huang J.

  Glycerophosphodiester phosphodiesterase (GDPD), which hydrolyzes glycerophosphodiesters into sn-glycerol-3-phosphate (G-3-P) and the corresponding alcohols, plays an important role in various physiological processes in both prokaryotes and eukaryotes. However, little is known about the physiologic ... >> More

  Glycerophosphodiester phosphodiesterase (GDPD), which hydrolyzes glycerophosphodiesters into sn-glycerol-3-phosphate (G-3-P) and the corresponding alcohols, plays an important role in various physiological processes in both prokaryotes and eukaryotes. However, little is known about the physiological significance of GDPD in plants. Here, we characterized the Arabidopsis GDPD family that can be classified into canonical GDPD (AtGDPD1-6) and GDPD-like (AtGDPDL1-7) subfamilies. In vitro analysis of enzymatic activities showed that AtGDPD1 and AtGDPDL1 hydrolyzed glycerolphosphoglycerol, glycerophosphocholine and glycerophosphoethanolamine, but the maximum activity of AtGDPD1 was much higher than that of AtGDPDL1 under our assay conditions. Analyses of gene expression patterns revealed that all AtGDPD genes except for AtGDPD4 were transcriptionally active in flowers and siliques. In addition, the gene family displayed overlapping and yet distinguishable patterns of expression in roots, leaves and stems, indicating functional redundancy as well as specificity of GDPD genes. AtGDPDs but not AtGDPDLs are up-regulated by inorganic phosphate (P(i) ) starvation. Loss-of-function of the plastid-localized AtGDPD1 leads to a significant decrease in GDPD activity, G-3-P content, P(i) content and seedling growth rate only under P(i) starvation compared with the wild type (WT). However, membrane lipid compositions in the P(i) -deprived seedlings remain unaltered between the AtGDPD1 knockout mutant and WT. Thus, we suggest that the GDPD-mediated lipid metabolic pathway may be involved in release of P(i) from phospholipids during P(i) starvation. << Less

  Plant J. 66:781-795(2011) [PubMed] [EuropePMC]

• Escherichia coli cytosolic glycerophosphodiester phosphodiesterase (UgpQ) requires Mg2+, Co2+, or Mn2+ for its enzyme activity.

  Ohshima N., Yamashita S., Takahashi N., Kuroishi C., Shiro Y., Takio K.

  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 specifi ... >> More

  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. << Less

  J. Bacteriol. 190:1219-1223(2008) [PubMed] [EuropePMC]

  This publication is cited by 3 other entries.

• Purification and characterization of glpQ-encoded glycerophosphodiester phosphodiesterase from Escherichia coli K-12.

  Larson T.J., van Loo-Bhattacharya A.T.

  Periplasmic glycerophosphodiester phosphodiesterase (EC 3.1.4.2) of Escherichia coli was purified seven-fold to near homogeneity from the cold osmotic shock fraction of a strain harboring a multicopy plasmid carrying the glpQ gene. The enzyme had a minimum subunit molecular weight of 40,000 as ass ... >> More

  Periplasmic glycerophosphodiester phosphodiesterase (EC 3.1.4.2) of Escherichia coli was purified seven-fold to near homogeneity from the cold osmotic shock fraction of a strain harboring a multicopy plasmid carrying the glpQ gene. The enzyme had a minimum subunit molecular weight of 40,000 as assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The native size of the enzyme was 70,000 as assessed by gel filtration chromatography and 75,000 as assessed by nondenaturing gradient polyacrylamide gel electrophoresis, indicating that the native state of the enzyme is dimeric. The enzyme hydrolyzed the deacylation products of all glycerophospholipids tested including glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol, glycerophosphoinositol, and glycerophosphoserine. The enzyme did not release glycerol or sn-glycerol 3-phosphate from phosphatidyl-DL-glycerol or lysophosphatidyl-DL-glycerol present in Triton X-100 micelles. The enzyme functioned optimally at pH 7.8. The enzyme was totally inactivated by dilution into 1 mM ethylenediaminetetraacetate or ethylene glycol bis(beta-aminoethyl ether)-N,N-tetraacetic acid. Activity was restored by the addition of Ca2+ or Cd2+, and was partially restored by the addition of Mn2+ or Cu2+. Co2+, Mg2+, Zn2+, and Fe2+ did not restore activity. The presence of calcium ions decreased the Km of the enzyme for the substrate, glycerophosphoglycerol, and increased the Vmax. << Less

  Arch. Biochem. Biophys. 260:577-584(1988) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.