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A novel NADPH-dependent carbonyl reductase of Candida macedoniensis: purification and characterization.
Arch Biochem Biophys. 1992 May 01; 294(2):469-74.AB

Abstract

A novel NADPH-dependent carbonyl reductase was purified to homogeneity from the soluble fraction of a cell extract of Candida macedoniensis AKU 4588. The enzyme catalyzes not only the reduction of quinones, but also the reduction of aromatic aldehydes, conjugated polyketones, 2'-ketopantothenate esters, and 4-chloro-3-oxobutanoate esters. The enzyme shows absolute specificity for NADPH as a coenzyme and also shows quite high affinity toward NADPH (Km less than 5 microM). The apparent Km values for menadione and p-toluquinone are 167 and 180 microM, respectively. The enzyme is not a flavoprotein and is a monomer protein with a relative molecular mass of 45,000. Dicoumarol, quercetin, and some sulfhydryl reagents inhibit the enzyme activity.

Authors+Show Affiliations

Department of Agricultural Chemistry, Kyoto University, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

1567202

Citation

Kataoka, M, et al. "A Novel NADPH-dependent Carbonyl Reductase of Candida Macedoniensis: Purification and Characterization." Archives of Biochemistry and Biophysics, vol. 294, no. 2, 1992, pp. 469-74.
Kataoka M, Doi Y, Sim TS, et al. A novel NADPH-dependent carbonyl reductase of Candida macedoniensis: purification and characterization. Arch Biochem Biophys. 1992;294(2):469-74.
Kataoka, M., Doi, Y., Sim, T. S., Shimizu, S., & Yamada, H. (1992). A novel NADPH-dependent carbonyl reductase of Candida macedoniensis: purification and characterization. Archives of Biochemistry and Biophysics, 294(2), 469-74.
Kataoka M, et al. A Novel NADPH-dependent Carbonyl Reductase of Candida Macedoniensis: Purification and Characterization. Arch Biochem Biophys. 1992 May 1;294(2):469-74. PubMed PMID: 1567202.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A novel NADPH-dependent carbonyl reductase of Candida macedoniensis: purification and characterization. AU - Kataoka,M, AU - Doi,Y, AU - Sim,T S, AU - Shimizu,S, AU - Yamada,H, PY - 1992/5/1/pubmed PY - 1992/5/1/medline PY - 1992/5/1/entrez SP - 469 EP - 74 JF - Archives of biochemistry and biophysics JO - Arch. Biochem. Biophys. VL - 294 IS - 2 N2 - A novel NADPH-dependent carbonyl reductase was purified to homogeneity from the soluble fraction of a cell extract of Candida macedoniensis AKU 4588. The enzyme catalyzes not only the reduction of quinones, but also the reduction of aromatic aldehydes, conjugated polyketones, 2'-ketopantothenate esters, and 4-chloro-3-oxobutanoate esters. The enzyme shows absolute specificity for NADPH as a coenzyme and also shows quite high affinity toward NADPH (Km less than 5 microM). The apparent Km values for menadione and p-toluquinone are 167 and 180 microM, respectively. The enzyme is not a flavoprotein and is a monomer protein with a relative molecular mass of 45,000. Dicoumarol, quercetin, and some sulfhydryl reagents inhibit the enzyme activity. SN - 0003-9861 UR - https://www.unboundmedicine.com/medline/citation/1567202/A_novel_NADPH_dependent_carbonyl_reductase_of_Candida_macedoniensis:_purification_and_characterization_ L2 - https://linkinghub.elsevier.com/retrieve/pii/0003-9861(92)90713-7 DB - PRIME DP - Unbound Medicine ER -