Kinetic and thermodynamic study of the reaction catalyzed by glucose-6-phosphate dehydrogenase with nicotinamide adenine dinucleotide

Campo, Julia S. Martín del; Patiño, Rodrigo

doi:10.1016/j.tca.2011.01.030

Cited by 4 publications

(1 citation statement)

References 16 publications

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“…Glucose-6-phosphate dehydrogenase (G6PD, EC 1.1.1.49, β -D-glucose-6-phosphate; NADP oxidoreductase) is the initial and the key regulatory enzyme in the pentose phosphate pathway [ 1 – 4 ]. It catalyzes the first step of the pentose phosphate pathway (PPP) [ 5 ] which is responsible for the production of NADPH and ribose-5-phosphate [ 6 ].…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Glucose-6-Phosphate Dehydrogenase from Camel Liver

et al. 2014

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Glucose-6-phosphate dehydrogenase from camel liver was purified to homogeneity by ammonium sulfate precipitation and a combination of DEAE-cellulose, Sephacryl S-300 gel filtration, and 2′, 5′ ADP Sepharose 4B affinity chromatography columns. The specific activity of camel liver G6PD is increased to 1.80438 units/mg proteins with 63-fold purification. It turned out to be homogenous on both native PAGE and 12% SDS PAGE, with a molecular weight of 64 kDa. The molecular weight of the native form of camel liver G6PD was determined to be 194 kDa by gel filtration indicating a trimeric protein. The K m value was found to be 0.081 mM of NADP+. Camel liver G6PD displayed its optimum activity at pH 7.8 with an isoelectric point (pI) of pH 6.6–6.8. The divalent cations MgCl2, MnCl2, and CoCl2 act as activators; on the other hand, CaCl2 and NiCl2 act as moderate inhibitors, while FeCl2, CuCl2, and ZnCl2 are potent inhibitors of camel liver G6PD activity. NADPH inhibited camel liver G6PD competitively with K i value of 0.035 mM. One binding site was deduced for NADPH on the enzyme molecule. This study presents a simple and reproducible purification procedure of G6PD from the camel liver.

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Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Glucose-6-Phosphate Dehydrogenase from Camel Liver

et al. 2014

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Biochemical Characterization of Buffalo Liver Glucose-6-Phosphate Dehydrogenase Isoforms

et al. 2015

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Glucose-6-phosphate dehydrogenase (G6PD) is a key regulatory enzyme involved in the pentose phosphate pathway. This works represents purification of two buffalo liver glucose-6-phosphate dehydrogenases (BLG6PD1 and BLG6PD2) using combination of ammonium sulfate precipitation and several chromatographic columns. Both enzymes (BLG6PD1 and BLG6PD2) were homogenous on both native PAGE as well as 12% SDS PAGE with molecular weights of 28 and 66 kDa. The molecular weight of BLG6PD1 and BLG6PD2 native forms were determined to be 28 and 66 kDa by gel filtration; indicating monomeric proteins. The K(m) values for BLG6PD1 and BLG6PD2 estimated to be 0.059 and 0.06 mM of β-nicotinamide adenine dinucleotide phosphate. The optimum activity of BLG6PD1 and BLG6PD2 were displayed at pH 8.0 and 8.2 with an isoelectric point (pI) of pH 7.7-7.9 and 5.7-5.9. The divalent cations MgCl2, and CoCl2 act as activators, on the other hand, FeCl2, CuCl2 and ZnCl2 are potent inhibitors of BLG6PD1 and BLG6PD2 activity. NADPH inhibited both isoenzymes competitively with Ki values of 0.012 and 0.030 mM. This study describes a reproducible purification scheme of G6PD from the liver of buffalo as a rich source.

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A system of co-immobilized dual-enzyme and coenzyme for in-situ coenzyme regeneration

Deng

Zhu²,

Jiao³

et al. 2022

Molecular Catalysis

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Kinetic and thermodynamic study of the reaction catalyzed by glucose-6-phosphate dehydrogenase with nicotinamide adenine dinucleotide

Cited by 4 publications

References 16 publications

Purification and Characterization of Glucose-6-Phosphate Dehydrogenase from Camel Liver

Purification and Characterization of Glucose-6-Phosphate Dehydrogenase from Camel Liver

Biochemical Characterization of Buffalo Liver Glucose-6-Phosphate Dehydrogenase Isoforms

A system of co-immobilized dual-enzyme and coenzyme for in-situ coenzyme regeneration

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