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Dual coenzyme activities of high-Km aldehyde dehydrogenase from rat liver mitochondria.
Biochem Cell Biol. 1990 Apr; 68(4):751-7.BC

Abstract

Various kinetic approaches were carried out to investigate kinetic attributes for the dual coenzyme activities of mitochondrial aldehyde dehydrogenase from rat liver. The enzyme catalyses NAD(+)- and NADP(+)-dependent oxidations of ethanal by an ordered bi-bi mechanism with NAD(P)+ as the first reactant bound and NAD(P)H as the last product released. The two coenzymes presumably interact with the kinetically identical site. NAD+ forms the dynamic binary complex with the enzyme, while the enzyme-NAD(P)H complex formation is associated with conformation change(s). A stopped-flow burst of NAD(P)H formation, followed by a slower steady-state turnover, suggests that either the deacylation or the release of NAD(P)H is rate limiting. Although NADP+ is reduced by a faster burst rate, NAD+ is slightly favored as the coenzyme by virtue of its marginally faster turnover rate.

Authors+Show Affiliations

Ottawa-Carleton Chemistry Institute, Carleton University, Ont., Canada.No affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

2223000

Citation

Tsai, C S., and D J. Senior. "Dual Coenzyme Activities of high-Km Aldehyde Dehydrogenase From Rat Liver Mitochondria." Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, vol. 68, no. 4, 1990, pp. 751-7.
Tsai CS, Senior DJ. Dual coenzyme activities of high-Km aldehyde dehydrogenase from rat liver mitochondria. Biochem Cell Biol. 1990;68(4):751-7.
Tsai, C. S., & Senior, D. J. (1990). Dual coenzyme activities of high-Km aldehyde dehydrogenase from rat liver mitochondria. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire, 68(4), 751-7.
Tsai CS, Senior DJ. Dual Coenzyme Activities of high-Km Aldehyde Dehydrogenase From Rat Liver Mitochondria. Biochem Cell Biol. 1990;68(4):751-7. PubMed PMID: 2223000.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Dual coenzyme activities of high-Km aldehyde dehydrogenase from rat liver mitochondria. AU - Tsai,C S, AU - Senior,D J, PY - 1990/4/1/pubmed PY - 1990/4/1/medline PY - 1990/4/1/entrez SP - 751 EP - 7 JF - Biochemistry and cell biology = Biochimie et biologie cellulaire JO - Biochem. Cell Biol. VL - 68 IS - 4 N2 - Various kinetic approaches were carried out to investigate kinetic attributes for the dual coenzyme activities of mitochondrial aldehyde dehydrogenase from rat liver. The enzyme catalyses NAD(+)- and NADP(+)-dependent oxidations of ethanal by an ordered bi-bi mechanism with NAD(P)+ as the first reactant bound and NAD(P)H as the last product released. The two coenzymes presumably interact with the kinetically identical site. NAD+ forms the dynamic binary complex with the enzyme, while the enzyme-NAD(P)H complex formation is associated with conformation change(s). A stopped-flow burst of NAD(P)H formation, followed by a slower steady-state turnover, suggests that either the deacylation or the release of NAD(P)H is rate limiting. Although NADP+ is reduced by a faster burst rate, NAD+ is slightly favored as the coenzyme by virtue of its marginally faster turnover rate. SN - 0829-8211 UR - https://www.unboundmedicine.com/medline/citation/2223000/Dual_coenzyme_activities_of_high_Km_aldehyde_dehydrogenase_from_rat_liver_mitochondria_ L2 - http://www.nrcresearchpress.com/doi/full/10.1139/o90-108?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -