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Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis.
Biochemistry. 1993 Mar 02; 32(8):2036-40.B

Abstract

A complete initial velocity study of the 6-phosphogluconate dehydrogenase from Candida utilis at pH 7 and 25 degrees C in both reaction directions suggests a rapid equilibrium random kinetic mechanism with dead-end E:NADP:(ribulose 5-phosphate) and E:NADPH:(6-phosphogluconate) complexes. Like substrate-product (NADP/NADPH and 6-phosphogluconate/ribulose 5-phosphate) pairs are competitive whatever the concentration of the other substrates but noncompetitive versus the other substrates, e.g., NADPH exhibits noncompetitive inhibition versus 6-phosphogluconate. This trend also holds true for all dead-end analogs, e.g., ATP-ribose is competitive versus NADP and noncompetitive versus 6-phosphogluconate. A quantitative analysis of the kinetic inhibition constants supports the assignment of kinetic mechanism. The ratio of the maximum velocities in the oxidative decarboxylation and reductive carboxylation directions is 75.

Authors+Show Affiliations

Department of Biochemistry, Texas College of Osteopathic Medicine, Fort Worth 76107.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8448161

Citation

Berdis, A J., and P F. Cook. "Overall Kinetic Mechanism of 6-phosphogluconate Dehydrogenase From Candida Utilis." Biochemistry, vol. 32, no. 8, 1993, pp. 2036-40.
Berdis AJ, Cook PF. Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis. Biochemistry. 1993;32(8):2036-40.
Berdis, A. J., & Cook, P. F. (1993). Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis. Biochemistry, 32(8), 2036-40.
Berdis AJ, Cook PF. Overall Kinetic Mechanism of 6-phosphogluconate Dehydrogenase From Candida Utilis. Biochemistry. 1993 Mar 2;32(8):2036-40. PubMed PMID: 8448161.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Overall kinetic mechanism of 6-phosphogluconate dehydrogenase from Candida utilis. AU - Berdis,A J, AU - Cook,P F, PY - 1993/3/2/pubmed PY - 1993/3/2/medline PY - 1993/3/2/entrez SP - 2036 EP - 40 JF - Biochemistry JO - Biochemistry VL - 32 IS - 8 N2 - A complete initial velocity study of the 6-phosphogluconate dehydrogenase from Candida utilis at pH 7 and 25 degrees C in both reaction directions suggests a rapid equilibrium random kinetic mechanism with dead-end E:NADP:(ribulose 5-phosphate) and E:NADPH:(6-phosphogluconate) complexes. Like substrate-product (NADP/NADPH and 6-phosphogluconate/ribulose 5-phosphate) pairs are competitive whatever the concentration of the other substrates but noncompetitive versus the other substrates, e.g., NADPH exhibits noncompetitive inhibition versus 6-phosphogluconate. This trend also holds true for all dead-end analogs, e.g., ATP-ribose is competitive versus NADP and noncompetitive versus 6-phosphogluconate. A quantitative analysis of the kinetic inhibition constants supports the assignment of kinetic mechanism. The ratio of the maximum velocities in the oxidative decarboxylation and reductive carboxylation directions is 75. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/8448161/Overall_kinetic_mechanism_of_6_phosphogluconate_dehydrogenase_from_Candida_utilis_ DB - PRIME DP - Unbound Medicine ER -