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Glyceraldehyde-3-phosphate Ferredoxin Oxidoreductase from Methanococcus Maripaludis

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Journal J Bacteriol
Specialty Microbiology
Date 2007 Aug 21
PMID 17704226
Citations 8
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Abstract

The genome sequence of the non-sugar-assimilating mesophile Methanococcus maripaludis contains three genes encoding enzymes: a nonphosphorylating NADP(+)-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPN), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR); all these enzymes are potentially capable of catalyzing glyceraldehyde-3-phosphate (G3P) metabolism. GAPOR, whose homologs have been found mainly in archaea, catalyzes the reduction of ferredoxin coupled with oxidation of G3P. GAPOR has previously been isolated and characterized only from a sugar-assimilating hyperthermophile, Pyrococcus furiosus (GAPOR(Pf)), and contains the rare metal tungsten as an irreplaceable cofactor. Active recombinant M. maripaludis GAPOR (GAPOR(Mm)) was purified from Escherichia coli grown in minimal medium containing 100 muM sodium molybdate. In contrast, GAPOR(Mm) obtained from cells grown in medium containing tungsten (W) and W and molybdenum (Mo) or in medium without added W and Mo did not display any activity. Activity and transcript analysis of putative G3P-metabolizing enzymes and corresponding genes were performed with M. maripaludis cultured under autotrophic conditions in chemically defined medium. The activity of GAPOR(Mm) was constitutive throughout the culture period and exceeded that of GAPDH at all time points. As GAPDH activity was detected in only the gluconeogenic direction and GAPN activity was completely absent, only GAPOR(Mm) catalyzes oxidation of G3P in M. maripaludis. Recombinant GAPOR(Mm) is posttranscriptionally regulated as it exhibits pronounced and irreversible substrate inhibition and is completely inhibited by 1 muM ATP. With support from flux balance analysis, it is concluded that the major physiological role of GAPOR(Mm) in M. maripaludis most likely involves only nonoptimal growth conditions.

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References
1.
Mukund S, Adams M . Molybdenum and vanadium do not replace tungsten in the catalytically active forms of the three tungstoenzymes in the hyperthermophilic archaeon Pyrococcus furiosus. J Bacteriol. 1996; 178(1):163-7. PMC: 177634. DOI: 10.1128/jb.178.1.163-167.1996. View

2.
Peterkofsky A, Gazdar C . Measurements of rates of adenosine 3':5'-cyclic monophosphate synthesis in intact Escherichia coli B. Proc Natl Acad Sci U S A. 1973; 70(7):2149-52. PMC: 433685. DOI: 10.1073/pnas.70.7.2149. View

3.
van der Oost J, Schut G, Kengen S, Hagen W, Thomm M, de Vos W . The ferredoxin-dependent conversion of glyceraldehyde-3-phosphate in the hyperthermophilic archaeon Pyrococcus furiosus represents a novel site of glycolytic regulation. J Biol Chem. 1998; 273(43):28149-54. DOI: 10.1074/jbc.273.43.28149. View

4.
Ballantine S, Boxer D . Nickel-containing hydrogenase isoenzymes from anaerobically grown Escherichia coli K-12. J Bacteriol. 1985; 163(2):454-9. PMC: 219143. DOI: 10.1128/jb.163.2.454-459.1985. View

5.
Rajagopalan K, Johnson J . The pterin molybdenum cofactors. J Biol Chem. 1992; 267(15):10199-202. View