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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The gnd gene, the structural gene for 6-phosphogluconate dehydrogenase, was sequenced and analyzed in 34 isolates from different serovars of the seven subspecies of Salmonella enterica to provide comparative information on the evolution in this gene, which has been studied extensively in Escherichia coli. The gene tree obtained by the neighbor-joining method in general gave separate branches for each subspecies, with the few exceptions readily explained by recombination. There is evidence of recombination involving transfer of long (more than 400 bp) and short (30-150 bp) segments of DNA. Four of the six long-segment transfers detected are at the 5' end of the gene, and in all four cases a variant of the chi sequence is located close to the recombination junction and appears to have mediated the recombination events. We suggest that in these four cases and in a fifth case with intersubspecies transfer of the whole gnd gene, the adjacent rfb (O antigen) locus may have been transferred in the same event. The estimates of the number of synonymous substitutions per synonymous site, KS, and the number of nonsynonymous substitutions per nonsynonymous site, KA, within the E. coli and S. enterica gnd genes, and also between the two species show an interesting distribution, with KS being lower toward the ends of the gene and KA in particular being lower in the first than in the second domain. In S. enterica, synonymous sites also seem to be subjected to negative selection. The ratio of KA to KS was higher within S. enterica and E. coli than between them, which may indicate that intraspecies variation is essentially between clones and that mildly deleterious mutations can be fixed within clones, which would thus raise KA within species.
Mol Biol Evol 1994 Nov
PMID:Molecular evolution in the gnd locus of Salmonella enterica. 781 22

Nucleotide sequences of portions of three plasmid genes (cib, cir, and abi) present in IncI1-ColIb colicin plasmids obtained from strains of Salmonella typhimurium isolated in either 1974 (Barker strains) or between 1935 and 1941 (Murray strains) were examined along with sequences of the chromosomal gene for 6-phosphogluconate dehydrogenase (gnd). Our principal findings were: (1) The plasmid genes were virtually identical to those in IncI1-ColIb plasmids from E. coli, suggesting that Salmonella and E. coli share overlapping pools of these plasmids. (2) The plasmid genes were much less polymorphic than gnd or any other known chromosomal gene from Salmonella, further suggesting horizontal transfer with rapid transmission and turnover. (3) No characteristic differences were found in either the plasmid genes or the chromosomal gene between the 1974 isolates and the Murray strains, indicating that these plasmids have been stable for at least several decades. (4) There was an excess of amino-acid replacement polymorphisms, relative to synonymous polymorphisms, in the plasmid genes, which is consistent with the hypothesis of diversifying selection among colicin-producing plasmid families. (5) The abi (abortive infection) gene present in each of the plasmids contained two single-nucleotide insertions relative to the published sequence. These result in a putative abi protein of 114 amino acids instead of 89.
J Mol Evol 1994 Aug
PMID:Genetic variation in IncI1-ColIb plasmids. 793 76

We have isolated and determined the nucleotide sequences for cDNA clones encoding glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) from the medfly Ceratitis capitata. The derived amino acid sequences for G6PD and 6PGD are presented and compared with G6PDs and 6PGDs from other species. The codon usage of the cDNA clones has little bias with the notable exceptions of arginine, glycine and leucine. The chromosomal location of the genes for 6PGD and G6PD were determined by in situ hybridization to salivary gland polytene chromosomes. This localization orients a genetic map of enzymatic loci and illustrates a remarkable similarity in the intra chromosomal order of homologous genes between Drosophila melanogaster and medfly.
Insect Mol Biol 1993
PMID:Isolation of cDNAs encoding 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase from the mediterranean fruit fly Ceratitis capitata: correlating genetic and physical maps of chromosome 5. 826

Effects of prolactin(Prl), bromocriptine(Br), testosterone propionate (TP), dihydrotestosterone (DHT) and combinations of these androgens with Prl/Br on the maximum catalytic capacities of seminal vesicular enzymes involved in the glycolytic and pentose phosphate pathways in castrated mature monkeys were studied. Castration decreased the activities of all of the enzymes studied such as hexokinase(HK), 6-phosphofructokinase(PFK), glyceraldehyde-3-phosphate dehydrogenase(G3PD), pyruvate kinase(PK), glucose 6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase(6PGD) in the seminal vesicles. Prl restored the activities of all of the enzymes to their normal values except G3PD. TP/DHT maintained all the enzyme activities at the normal tissue intact level. Prl given along with androgens further enhanced the androgen action with regard to all the enzymes activities except G3PD. Br decreased all of the enzymes but Br with androgens maintained all the enzyme activities at the normal level. Castration decreased significantly serum T/DHT titres but Prl did not alter Prl levels. Prl+TP/DHT elevated Prl levels. Br alone decreased serum Prl, T and DHT titres, but Br+TP/DHT decreased only Prl, elevated T and maintained DHT levels. These results suggest that Prl has a direct as well as a synergistic action with androgens on the activities of the enzymes of glycolysis and pentose phosphate pathways in the seminal vesicles of castrated monkeys.
Biochem Mol Biol Int 1993 Oct
PMID:Effects of prolactin and androgens on enzymes of carbohydrate metabolism in seminal vesicles of castrated mature bonnet monkeys, Macaca radiata. 827 11

The human leukaemic cell line HL60 undergoes differentiation to granulocyte-like cells in response to dimethylsulphoxide (DMSO). The rates of glucose and glutamine utilization were studied in HL60 cells that were either undifferentiated or fully differentiated by 9 days exposure to DMSO. Differentiation did not alter the rate of utilization of exogenous glucose, approximately 75% of which was converted to lactate in each case. The activities of hexokinase, phosphofructokinase, pyruvate kinase and citrate synthase were similarly unaffected. In contrast, the activity of the oxidative segment of the pentose-phosphate pathway was enhanced by differentiation, and no glycogen synthase activity could be detected. These observations are consistent with the significantly lower content of glycogen, the increased activities of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase and the increased oxidation of [1-14C] glucose relative to [6-14C] glucose in the differentiated cells. Glucose utilization was depressed by exogenous glutamine but, at the same time, glutamine utilization was enhanced by glucose in both cell types; these reciprocal effects were more pronounced in the undifferentiated HL60 cells. Glucose utilization may be depressed in the presence of glutamine as a result of the allosteric inhibition of a rate-limiting step of glycolysis (eg. phosphofructokinase). In spite of having glutaminase activity twice that of their differentiated counterparts, the uptake of glutamine by undifferentiated HL60 cells was low, especially when it was the sole substrate. The stimulation of glutaminolysis by glucose may be due to activation of mitochondrial glutamine transport. A large proportion of the glutamine utilized by both cells contributed to a net accumulation of glutamate, aspartate and alanine, whilst up to 35% was oxidized to CO2. In contrast, almost all of the glucose utilized was converted to lactate and very little was oxidized. The high rates of glycolysis and glutaminolysis observed before and after differentiation may not contribute primarily to energy production but may supply, in undifferentiated cells, substrates for biosynthetic processes that generate nucleic acid precursors or, in the case of differentiated cells which synthesize reactive oxygen intermediates, substrates that maintain NADP in a reduced state.
Biochem Mol Biol Int 1993 Apr
PMID:Glycolytic, glutaminolytic and pentose-phosphate pathways in promyelocytic HL60 and DMSO-differentiated HL60 cells. 833 14

We have obtained well-ordered single crystals of 6-phosphogluconate dehydrogenase, an enzyme of the oxidative branch of the pentose phosphate pathway, from Trypanosoma brucei. The crystals are trigonal rhombs with unit cell dimensions a = b = 135.1 A, c = 116.7 A and belong to one of the enantiomorphic pair of space groups P3(1)21/P3(2)21. X-ray diffraction to better than 2.8 A has been recorded using a rotating anode CuK alpha source. Elucidation of the three-dimensional structure of the T. brucei enzyme will, by indicating structural differences from the known sheep enzyme structure, aid the design of mutants to probe the active site. Knowledge of the structure will also assist in assessing the potential use of rationally designed compounds to inhibit this enzyme specifically.
J Mol Biol 1993 Sep 20
PMID:Preliminary crystallographic study of 6-phosphogluconate dehydrogenase from Trypanosoma brucei. 837 7

A Trypanosoma brucei gene encoding 6-phosphogluconate dehydrogenase (6-PGDH) (EC 1.1.1.44) was identified and cloned by functional complementation of Escherichia coli gnd mutants with genomic trypanosome DNA. The T. brucei gnd gene is present as a single copy. In Northern blot experiments a probe derived from the gene hybridises to 2 transcripts (2.9 kb and 3.1 kb) which are found in both bloodstream and procyclic form organisms; the larger transcript is more abundant in bloodstream form organisms. The derived amino acid sequence of the protein is 479 amino acids in length, with a molecular weight of 52,000. It is homologous to 6-PGDHs from bacterial and mammalian sources, but diverges significantly from these other enzymes.
Mol Biochem Parasitol 1993 Jan
PMID:A 6-phosphogluconate dehydrogenase gene from Trypanosoma brucei. 842 18

Natural hybrid zones are known to have unusually high levels of novel or otherwise rare electrophoretic variants (the "rare allele phenomenon"). These variant alleles are most likely the result either of high levels of unique mutations in hybrids or of intragenic recombination between divergent alleles from the parental populations. This study uses DNA sequence comparisons to determine which process has produced a rare allele of the 6-phosphogluconate dehydrogenase (6-PGD) gene in a subspecific hybrid zone of the California field mouse (Peromyscus californicus). About 70% of the coding sequence of 6-PGD was cloned and sequenced from three alleles, including two widespread alleles and one rare allele unique to hybrid populations. Sequence comparisons among the three alleles reveal no patterns that would indicate that the variant was formed by intragenic recombination. Instead, the unique allele of 6-PGD studied seems to have developed by the accumulation of base substitutions, which supports the hypothesis of increased mutation rates in hybrids.
J Mol Evol 1995 Dec
PMID:The molecular mechanism underlying the "rare allele phenomenon" in a subspecific hybrid zone of the California field mouse, Peromyscus californicus. 858 12

Bromopyruvate inactivates 6-phosphogluconate dehydrogenase by affinity labeling. Kinetic analyses, stoichiometry and isolation of a single labelled tryptic peptide of the modified protein indicate that inactivation is due to the affinity labeling of a single cysteine residue, identified as cysteine 401. It thus appears that this cysteine is within a short distance from the protein site involved in the binding of the carboxylate group of the substrate. These results suggest that the carboxylate binding site of proteins could be used as an anchorage point for affinity labeling, and that bromopyruvate can be used to individuate an amino acid residue within few A from this site.
Biochem Mol Biol Int 1995 Nov
PMID:Bromopyruvate for the affinity labelling of a single cysteine residue near the carboxylate binding site of lamb liver 6-phosphogluconate dehydrogenase. 858 52

Earlier work from this laboratory has determined that glucose plays an important role in the mechanisms regulating meiotic maturation in mammalian oocytes. In the current study, we have further explored the role of glucose in hormone-induced germinal vesicle breakdown (GVB) in an effort to better understand how glucose utilization and metabolism relate to the control of meiotic maturation in mouse cumulus cell-enclosed oocytes (CEO). When CEO were cultured in medium containing 4 mM hypoxanthine (to maintain meiotic arrest), 5.5 mM glucose, and 0.23 mM pyruvate, follicle-stimulating hormone (FSH) stimulated lactate accumulation in a time-dependent manner. Addition of 2-deoxyglucose (2-DG) to the medium at various times after the initiation of culture resulted in rapid termination of lactate production and suppression of FSH-induced GVB scored after 18 hr of culture, the effectiveness diminishing the longer the delay before addition of 2-DG. By 8 hr, addition of 2-DG was without effect on GVB. Similar effects were seen when FSH-treated CEO were washed free of glucose. In a 2-DG dose-response experiment, gonadotropin-induced lactate production was prevented, but this inhibition did not necessarily prevent GVB. The activities of six metabolic enzymes were measured in extracts of freshly isolated complexes, and in order of increasing activity were: hexokinase, 6-phosphogluconate dehydrogenase, glucose-6-phosphate dehydrogenase, phosphofructokinase, lactate dehydrogenase, and pyruvate kinase. Of the six enzymes examined, only hexokinase activity was increased in CEO exposed to FSH. CEO were cultured in microdrops in the presence or absence of FSH, and aliquots from the same microdrop were assayed for glucose, lactate, and pyruvate. In response to FSH, utilization of glucose in microdrop cultures by CEO was markedly increased and was accompanied by comparable lactate production and limited pyruvate production. Cycloheximide and alpha-amanitin both blocked FSH-induced oocyte maturation, but only cycloheximide prevented the increase in hexokinase activity and glucose consumption. These data suggest that hexokinase is an important rate-limiting enzyme for glucose utilization that is under translational control and participates in the mechanisms controlling the reinitiation of meiosis. However, stimulation of glycolytic activity does not appear to be a necessary concomitant for meiotic induction.
Mol Reprod Dev 1996 May
PMID:Glucose utilization during gonadotropin-induced meiotic maturation in cumulus cell-enclosed mouse oocytes. 872


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