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Kinetic studies of Haemophilus influenzae 6-phosphogluconate dehydrogenase.
Biochim Biophys Acta. 1989 Jan 19; 994(1):75-80.BB

Abstract

Haemophilus influenzae 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating), EC 1.1.1.44) was purified 308-fold to electrophoretic homogeneity with a 16% recovery through a five-step procedure involving salt fractionation and hydrophobic and affinity chromatography. The purified enzyme was demonstrated to be a dimer of Mr 70,000, and to catalyze a sequential reaction process. The enzyme was NADP-specific and kinetic parameters for the oxidation of 6-phosphogluconate were determined for NADP and four structural analogs of NADP. Coenzyme-competitive inhibition by adenosine derivatives was significantly enhanced by the presence of a 2'-phosphoryl group consistent with the observed coenzyme specificity of the enzyme. The purified enzyme was effectively inhibited by 3-aminopyridine adenine dinucleotide phosphate, but at concentrations higher than that observed to inhibit growth of the organism. Rates of inactivation of the enzyme by N-ethylmaleimide were suggestive of sulfhydryl involvement in the reaction catalyzed.

Authors+Show Affiliations

Department of Biochemistry and Nutrition, Virginia Polytechnic Institute and State University Blacksburg 24061.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

2783298

Citation

Yoon, H, et al. "Kinetic Studies of Haemophilus Influenzae 6-phosphogluconate Dehydrogenase." Biochimica Et Biophysica Acta, vol. 994, no. 1, 1989, pp. 75-80.
Yoon H, Anderson CD, Anderson BM. Kinetic studies of Haemophilus influenzae 6-phosphogluconate dehydrogenase. Biochim Biophys Acta. 1989;994(1):75-80.
Yoon, H., Anderson, C. D., & Anderson, B. M. (1989). Kinetic studies of Haemophilus influenzae 6-phosphogluconate dehydrogenase. Biochimica Et Biophysica Acta, 994(1), 75-80.
Yoon H, Anderson CD, Anderson BM. Kinetic Studies of Haemophilus Influenzae 6-phosphogluconate Dehydrogenase. Biochim Biophys Acta. 1989 Jan 19;994(1):75-80. PubMed PMID: 2783298.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Kinetic studies of Haemophilus influenzae 6-phosphogluconate dehydrogenase. AU - Yoon,H, AU - Anderson,C D, AU - Anderson,B M, PY - 1989/1/19/pubmed PY - 1989/1/19/medline PY - 1989/1/19/entrez SP - 75 EP - 80 JF - Biochimica et biophysica acta JO - Biochim. Biophys. Acta VL - 994 IS - 1 N2 - Haemophilus influenzae 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate:NADP+ 2-oxidoreductase (decarboxylating), EC 1.1.1.44) was purified 308-fold to electrophoretic homogeneity with a 16% recovery through a five-step procedure involving salt fractionation and hydrophobic and affinity chromatography. The purified enzyme was demonstrated to be a dimer of Mr 70,000, and to catalyze a sequential reaction process. The enzyme was NADP-specific and kinetic parameters for the oxidation of 6-phosphogluconate were determined for NADP and four structural analogs of NADP. Coenzyme-competitive inhibition by adenosine derivatives was significantly enhanced by the presence of a 2'-phosphoryl group consistent with the observed coenzyme specificity of the enzyme. The purified enzyme was effectively inhibited by 3-aminopyridine adenine dinucleotide phosphate, but at concentrations higher than that observed to inhibit growth of the organism. Rates of inactivation of the enzyme by N-ethylmaleimide were suggestive of sulfhydryl involvement in the reaction catalyzed. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/2783298/Kinetic_studies_of_Haemophilus_influenzae_6_phosphogluconate_dehydrogenase_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0167-4838(89)90064-2 DB - PRIME DP - Unbound Medicine ER -