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Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from a methanol-utilizing yeast, Candida boidinii.
Biochim Biophys Acta. 1979 Jan 12; 566(1):1-11.BB

Abstract

Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP oxidoreductase, EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP oxidoreductase, EC 1.1.1.44) were purified approx. 1700 fold and 330 fold, respectively, from Candida boidinii grown on methanol. The final enzyme preparations were homogeneous as judged by polyacrylamide gel electrophoresis. The molecular weights of the enzymes were estimated to be 118 000 and 110 000, respectively. Both enzymes are composed of two probably identical subunits and the molecular weights of the polypeptide chains were calculated to be 61 000 and 58 000, respectively. From a consideration of enzyme activities and types of inhibition by different metabolites the role of these two enzymes in glucose- and methanol-metabolism is discussed.

Authors

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Pub Type(s)

Journal Article

Language

eng

PubMed ID

31936

Citation

Kato, N, et al. "Purification and Properties of Glucose-6-phosphate Dehydrogenase and 6-phosphogluconate Dehydrogenase From a Methanol-utilizing Yeast, Candida Boidinii." Biochimica Et Biophysica Acta, vol. 566, no. 1, 1979, pp. 1-11.
Kato N, Sahm H, Schütte H, et al. Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from a methanol-utilizing yeast, Candida boidinii. Biochim Biophys Acta. 1979;566(1):1-11.
Kato, N., Sahm, H., Schütte, H., & Wagner, F. (1979). Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from a methanol-utilizing yeast, Candida boidinii. Biochimica Et Biophysica Acta, 566(1), 1-11.
Kato N, et al. Purification and Properties of Glucose-6-phosphate Dehydrogenase and 6-phosphogluconate Dehydrogenase From a Methanol-utilizing Yeast, Candida Boidinii. Biochim Biophys Acta. 1979 Jan 12;566(1):1-11. PubMed PMID: 31936.
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TY - JOUR T1 - Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from a methanol-utilizing yeast, Candida boidinii. AU - Kato,N, AU - Sahm,H, AU - Schütte,H, AU - Wagner,F, PY - 1979/1/12/pubmed PY - 1979/1/12/medline PY - 1979/1/12/entrez SP - 1 EP - 11 JF - Biochimica et biophysica acta JO - Biochim Biophys Acta VL - 566 IS - 1 N2 - Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP oxidoreductase, EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP oxidoreductase, EC 1.1.1.44) were purified approx. 1700 fold and 330 fold, respectively, from Candida boidinii grown on methanol. The final enzyme preparations were homogeneous as judged by polyacrylamide gel electrophoresis. The molecular weights of the enzymes were estimated to be 118 000 and 110 000, respectively. Both enzymes are composed of two probably identical subunits and the molecular weights of the polypeptide chains were calculated to be 61 000 and 58 000, respectively. From a consideration of enzyme activities and types of inhibition by different metabolites the role of these two enzymes in glucose- and methanol-metabolism is discussed. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/31936/Purification_and_properties_of_glucose_6_phosphate_dehydrogenase_and_6_phosphogluconate_dehydrogenase_from_a_methanol_utilizing_yeast_Candida_boidinii_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0005-2744(79)90242-0 DB - PRIME DP - Unbound Medicine ER -