Glucose-6-phosphate dehydrogenase (G6PD; d-glucose 6-phosphate: NADP+ oxidoreductase, EC 1.1.1.49) has been purified from Aspergillus nidulans and Aspergillus niger by a combination of affinity and anion exchange chromatography. A 500–1000-fold purification was obtained and the final enzyme preparations were shown to be pure but not homogeneous. For both fungi the purified enzyme preparation gave two bands on native and denaturing gels. The catalytically active form is a multimer. The molecular mass of the monomers is 60 and 57 kDa for A. nidulans and 55 and 53 kDa for A. niger. Both enzymes exhibited strict specificity towards both substrates glucose 6-phosphate and NADP+. The A. nidulans and A. niger G6PD enzymes catalyse the conversion of glucose 6-phosphate via a random order mechanism. Inhibition studies provided evidence for the physiological role of G6PD as producer of NADPH in both fungi.
BainbridgeB. W.,
BullA. T.,
PirtS. J.,
RowleyB. I.,
TrinciA. P.1971; Biochemical and structural changes in non-growing and autolysing cultures of Aspergillus nidulans. Transactions of the British Mycological Society 56:371–375
BeutlerE.,
KuhlW.1986; Characteristics and significance of the reverse glucose-6-phosphate dehydrogenase reaction. Journal of Laboratory and Clinical Medicine 107:502–507
BonsignoreA.,
De FloraA.1972; Regulatory properties of glucose-6-phosphate dehydrogenase. In Current Topics in Cellular Regulation6 pp. 21–62HoeckerB. L.,
StadtmanE. R.
Edited by New York: Academic Press;
CamardellaL.,
CarusoC.,
RutiglianoB.,
RomanoM.,
Di PriscoG.,
Descalzi-Cancedda.
1988; Human erythrocyte glucose-6-phosphate dehydrogenase. Identification of a reactive lysyl residue, labelled with 5′-pyridoxal phosphate. European Journal of Biochemistry 171:485–489
CarterB. L. A.,
BullA. T.1969; Studies of fungal growth and intermediary carbon metabolism and non-steady-state conditions. Biotechnology and Bioengineering 11:785–804
Cébrian-PérezJ. A.,
Muiño-BlancoT.,
Pérez-MartosA.,
López-PérezM. J.1989; Characterisation of three enzymatic forms of glucose-6-phosphate dehydrogenase from Aspergillus oryzae. Revista Espanola de Fisiologica 45:271–276
DearrigaD.,
MonteroS.,
BustoF.,
SolerJ.1986; Partial purification and some kinetic properties of glucose-6-phosphate dehydrogenase from Phycomyces blakesleanus. Biochimie 68:293–302
DijkemaC.,
KesterH. C. M.,
VisserJ.1985; 13C-NMR studies on carbon metabolism in the hyphal fungus Aspergillus nidulans. Proceedings of the National Academy of Sciences of the United States of America 82:14–18
DijkemaC.,
Pels RijckenR.,
KesterH. C. M.,
VisserJ.1986; 13C-NMR studies on the influence of pH and nitrogen source on the polyol pool formation in Aspergillus nidulans. FEMS Microbiology Letters 33:125–131
GoosenT.,
BosC. J.,
Van Den BroekH. W. J.1992; Transformation and gene manipulation in filamentous fungi; an overview. In Handbook of Applied Mycology4 Fungal Biotechnology pp. 151–195AroraD. K.,
ElanderR. P.,
MukerjiK. G.
Edited by New York: Marcel Dekker;
HammondJ. B. W.1985; Glucose-6-phosphate dehydrogenase from Agaricus bisporus: purification and properties. Journal of General Microbiology 131:321–328
HoltenD.,
ProscalD.,
ChangH.-L.1976; Regulation of the pentose phosphate pathway by the NADP+/NADPH ratio. Biochemical and Biophysical Research Communications 68:436–441
Van Den HondelC.A.M.M.J.,
PuntP. J.,
Van GorcomR. F. M.1992; Production of extracellular proteins by the filamentous fungus Aspergillus. Antonie van Leeuwenhoek 61:153–160
HultK. A.,
GatenbeckS.1978; Production of NADPH in the mannitol cycle and its relation to polyketide formation in Alternaria alternata. European Journal of Biochemistry 88:607–612
JagannathanV.,
RangachariP. N.,
DamodaranM.1956; Carbohydrate metabolism in citric acid fermentation. 5. Purification and properties of Zwischenferment from A. niger. Biochemical Journal 64:477–481
JefferyJ.,
HobbsL.,
JornvallH.1985; Glucose-6-phosphate dehydrogenase from S. cerevisiae: characterization of a reactive lysine residue labelled with acetylsalicylic acid. Biochemistry 24:666–671
KahnA.,
BoivinP.,
RubinsonH.,
CottreauD.,
MarieJ.,
DreyfusJ.-C.1976; Modification of purified glucose-6-phosphate dehydrogenase and other enzymes by a factor of low molecular weight in some leukemic cells. Proceedings of the National Academy of Sciences of the United States of America 73:77–81
LevyH. R.,
CookC.1991; Purification and properties of NADP-linked glucose-6-phosphate dehydrogenase from Acetobacter hansenii (Acetobacter xylinium). Archives of Biochemistry and Biophysics 291:161–167
LöhrG. W.,
WallerH. D.1974; Glucose-6-phosphate dehydrogenase. In Methoden der enzymatischen Analyse1 pp. 673–681BergmeyerH. U.
Edited by Weinheim: Verlag Chemie GMBH;
McculloughW.,
PaytonM. A.,
RobertsC. F.1977; Carbon metabolism in Aspergillus nidulans. In Genetics and Physiology of Aspergillus pp. 97–129SmithJ. E.,
PatemanJ. A.
Edited by New York: Academic Press;
MalathiS.,
ShanmugasundaramE. R. B.1987; Studies on the isolation of glucose-6-phosphate dehydrogenase from A. nidulans. Journal of the Indian Institute of Sciences 7:43–46
MatsuokaN.1988; Purification of glucose-6-phosphate dehydrogenase from the sea-urchin Hemicentrotus pulcherrimus. Comparative Biochemistry and Physiology 89B:517–520
Muiño-BlancoT.,
Cébrian-PérezJ. A.,
Pérez-MartosA.1983; Regulation of the oxidative phase of the pentose phosphate pathway in Aspergillus oryzae (Ahlburg). Archives of Microbiology 136:39–41
NiehausW. G.,
DiltsR. P.1984; Purification of glucose-6-phosphate dehydrogenase from Aspergillus parasiticus. Archives of Biochemistry and Biophysics 228:113–119
NishikawaK.,
KuwanaH.1985; Deficiency of glucose-6-phosphate dehydrogenase in ace-7 strains of Neurospora crassa. Japanese Journal of Genetics 60:39–52
OuchterlonyO.,
NilsonL. A.1978; Immunodiffusion and immuno-electrophoresis. In Handbook of Experimental Immunology, 3rd edn. pp. 1911–1944WeinD. M.
Edited by Oxford: Blackwell Scientific Publications;
ReuterR.,
NaumannM.,
GüttelK.,
HofmannE.1986; Interactions of immobilized and free triazine dyes with glucose-6-phosphate dehydrogenase from yeast. Biomedica Biochemica Acta 45:273–280
RöberB.,
StolleJ.,
ReuterG.1984; Eigenschaften der Glucose-6-phosphat Dehydrogenase aus der SCP Hefe Candida maltosa H. Zeitschrift für allgemeine Mikrobiologie 24:629–636
ScottW. A.,
TatumE. L.1970; Glucose-6-phosphate dehydrogenase and Neurospora morphology. Proceedings of the National Academy Sciences of the United States of America 66:515–522
ScottW. A.,
MahonyE.1976; Defects of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in Neurospora and their pleiotropic effects. Current Topics in Cellular Regulation 10:205–236
SinghM.,
ScruttonN. S.,
ScruttonM. C.1988; NADPH generation in A. nidulans: is the mannitol cycle involved?. Journal of General Microbiology 134:643–654
UitzetterJ.H.A.A.1982Studies on the carbon metabolism in wild type and mutants of Aspergillus nidulans Thesis Agricultural University Wageningen; The Netherlands:
VincenziniM. T.,
VanniP.,
HanozetG. M.,
ParentiP.,
GuerritoreA.1986; Inactivation and degradation of yeast glucose-6-phosphate dehydrogenase selectively modified by pyridoxal-5-phosphate. Enzyme 36:239–246