Hydrogen-transfer reactions catalyzed by pyridine nucleotide linked dehydrogenases

Allison, William S.; White, Harold B.; Connors, Michael J.

doi:10.1021/bi00788a017

Cited by 12 publications

(5 citation statements)

References 21 publications

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“…Coenzyme stereospecificity. [4-3H]NAD+ was prepared essentially by the enzymatic procedure of Allison et al (1). In this procedure [4B-'H]NADH was prepared by stereospecifically reducing NAD+ with glyceraldehyde-3-phosphate dehydrogenase in the presence of [1-3H ]glyceraldehyde-3-phosphate, which was generated from [1-3H Idihydroxyacetone phosphate by triose phosphate isomerase (1).…”

Section: Methodsmentioning

confidence: 99%

“…[4-3H]NAD+ was prepared essentially by the enzymatic procedure of Allison et al (1). In this procedure [4B-'H]NADH was prepared by stereospecifically reducing NAD+ with glyceraldehyde-3-phosphate dehydrogenase in the presence of [1-3H ]glyceraldehyde-3-phosphate, which was generated from [1-3H Idihydroxyacetone phosphate by triose phosphate isomerase (1). The stereospecific labeling of NADH was then doubly confirmed by reoxidizing it with fl-hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides, a B-specific enzyme, and supernatant malate dehydrogenase from pig heart.…”

Section: Methodsmentioning

confidence: 99%

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Purification and properties of malate dehydrogenase from Pseudomonas testosteroni

You¹,

Kaplan²

1975

J Bacteriol

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Nicotinamide adenine dinucleotide-linked malate dehydrogenase has been purified from Pseudomonas testosteroni (ATCC 11996). The purification represents over 450-fold increase in specific activity. The amino acid composition of the enzyme was determined and found to be quite different from the composition of the malate dehydrogenases from animal sources as well as from Escherichia coli. Despite this difference, however, the data show that the enzymatic properties of the purified enzyme are remarkably similar to those of other malate dehydrogenases that have been previously studied. The Pseudomonas enzyme has a molecular weight of 74,000 and consists of two subunits of identical size. In addition to L-malate, the enzyme slowly oxidizes other four-carbon dicarboxylates having an a-hydroxyl group of S configuration such as meso-and (-)-tartrate. Rate-determining steps, which differ from that of the reaction involving L-malate, are discussed for the reaction involving these alternative substrates. Oxidation of hydroxymalonate, a process previously undetected with other malate dehydrogenases, is demonstrated fluorometrically. Hydroxymalonate and D-malate strongly enhance the fluorescence of the reduced nicotinamide adenine dinucleotide bound to the enzyme. The enzyme is A-stereospecific with respect to the coenzyme. Malate dehydrogenase is present in a single form in the Pseudomonas. The susceptibility of the enzyme to activation or inhibition by its substrates-particularly the favoring of the oxidation of malate at elevated concentrations-strongly resembles the properties of the mitochondrial enzymes. The present study reveals that whereas profound variations in chemical composition have occurred between the prokaryotic and eukaryotic enzymes, the physical and catalytic properties of malate dehydrogenase, unlike lactate dehydrogenase, are well conserved during the evolutionary process.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Purification and properties of malate dehydrogenase from Pseudomonas testosteroni

You¹,

Kaplan²

1975

J Bacteriol

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mentioning

confidence: 95%

“…[15] The 2 H NMR spectrum of the mixture indicated that the deuterium atom is attached exclusively at the C4 position (d 3.18). Therefore, in the model reactions, the reactive hydrogen atom of 1 is transferred to the C4 position of NAD model compounds 2 a ± d. This process is comparable to the direct hydrogen transfer [16] Finally, we performed sequential GAPDH-and LDH-type model reactions in a one-pot reaction (Scheme 2). After removal of the THF solvent, the crude deuterated dihydro-nicotinamides (3 a, [D 1 ]-3 a, and [D 2 ]-3 a) from the GAPDHtype reaction of 2 a with [D 1 ]-1 (5 equiv) were used for the following LDH-type reaction with methyl benzoylformate (5 (5 equiv) in acetonitrile without further addition of Mg 2 .…”

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confidence: 99%

Biomimetic Oxidation of Aldehyde with NAD+ Models: Glycolysis-Type Hydrogen Transfer in an NAD+/NADH Model System

Kanomata

Suzuki

Yoshida

et al. 1998

Angewandte Chemie International Edition

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Just like in biological systems, the GAPDH-catalyzed oxidation of aldehyde to carboxylate proceeds in conjunction with 1,4-selective reduction of NAD to NADH model compounds [Eq. (1)]. The combination of GAPDH- and LDH-type transfer reactions is also described here as a system mimic for the NAD /NADH redox cycle in anaerobic glycolysis. GAPDH=D-glyceraldehyde-3-phosphate dehydrogenase, LDH=L-lactate dehydrogenase.

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“…8 und 10), was vermutlich auf eine Isomerisierung von 3 c,d zu 4 c,d in Gegenwart der Pyridinium-Salze 2 c,d zurückzuführen ist. [14] Durch ein Isotopen-Experiment konnte eindeutig bestätigt werden, daû diese Selektivitäten kinetisch kontrolliert sind: übertragung [16] von der Thiohemiacetal-Zwischenstufe auf das Coenzym NAD in der natürlichen GAPDH-Oxidation ähnlich.…”

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Biomimetische Oxidation von Aldehyden mit NAD+-Modellverbindungen – Wasserstoffübertragung vom Glycolyse-Typ in einem NAD+/NADH-Modellsystem

et al. 1998

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Hydrogen-transfer reactions catalyzed by pyridine nucleotide linked dehydrogenases

Cited by 12 publications

References 21 publications

Purification and properties of malate dehydrogenase from Pseudomonas testosteroni

Purification and properties of malate dehydrogenase from Pseudomonas testosteroni

Biomimetic Oxidation of Aldehyde with NAD+ Models: Glycolysis-Type Hydrogen Transfer in an NAD+/NADH Model System

Biomimetische Oxidation von Aldehyden mit NAD+-Modellverbindungen – Wasserstoffübertragung vom Glycolyse-Typ in einem NAD+/NADH-Modellsystem

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