Interactions of 3-Aminopyridine Adenine Dinucleotide with Dehydrogenases

Fisher, Tom Lyons; Vercellotti, Sharon V.; Anderson, Bruce M.

doi:10.1016/s0021-9258(19)43771-x

Cited by 66 publications

(8 citation statements)

References 20 publications

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“…Reagents. 3-Aminopyridine adenine dinucleotide was synthesized by the method of Fisher et al (1973). Deazaflavin (7, was the gift from the late Dr. P. Hemmerich.…”

Section: Methodsmentioning

confidence: 99%

Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (Il84Y) in the pyridine nucleotide binding domain

Maeda-Yorita¹,

Russell²,

Guest³

et al. 1991

Biochemistry

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The binding of pyridine nucleotide to human erythrocyte glutathione reductase, an enzyme of known three-dimensional structure, requires some movement of the side chain of Tyr197. Moreover, this side chain lies very close to the isoalloxazine ring of the FAD cofactor. The analogous residue, Ile184, in the homologous enzyme Escherichia coli lipoamide dehydrogenase has been altered by site-directed mutagenesis to a tyrosine residue (I184Y) [Russell, G. C., Allison, N., Williams, C. H., Jr., & Guest, J.R. (1989) Ann. N.Y. Acad. Sci. 573, 429-431]. Characterization of the altered enzyme shows that the rate of the pyridine nucleotide half-reaction has been markedly reduced and that the spectral properties have been changed to mimic those of glutathione reductase. Therefore, Ile184 is shown to be an important residue in modulating the properties of the flavin in lipoamide dehydrogenase. Turnover in the dihydrolipoamide/NAD+ reaction is decreased by 10-fold and in the NADH/lipoamide reaction by 2-fold in I184Y lipoamide dehydrogenase. The oxidized form of I184Y shows remarkable changes in the fine structure of the visible absorption and circular dichroism spectra and also shows nearly complete quenching of FAD fluorescence. The spectral properties of the altered enzyme are thus similar to those of glutathione reductase and very different from those of wild-type lipoamide dehydrogenase. On the other hand, spectral evidence does not reveal any change in the amount of charge-transfer stabilization at the EH2 level. Stopped-flow data indicate that, in the reduction of I184Y by NADH, the first step, reduction of the flavin, is only slightly slowed but the subsequent two-electron transfer to the disulfide is markedly inhibited.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…Reagents. 3-Aminopyridine adenine dinucleotide was synthesized by the method of Fisher et al (1973). Deazaflavin (7, was the gift from the late Dr. P. Hemmerich.…”

Section: Methodsmentioning

confidence: 99%

Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (Il84Y) in the pyridine nucleotide binding domain

Maeda-Yorita¹,

Russell²,

Guest³

et al. 1991

Biochemistry

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“…The possibility of the nonenzymatic formation of a pyridine dinucleotide-Kepone complex was investigated by studying the fluorescence of 3-aminopyridine adenine dinucleotide. This fluorescing dinucleotide has been shown to be a sensitive indicator of charge-transfer complex formation with halogens (Fisher et al, 1973) which results in the extensive quenching of the fluorescence of the pyridinium moiety of this compound. At concentrations causing effective inhibition of lactate and malate dehydrogenases, no quenching of the fluorescence of 3aminopyridine adenine dinucleotide was observed, suggesting no appreciable complex formation.…”

Section: Discussionmentioning

confidence: 99%

“…A sample of Kepone was generously supplied by Allied Chemical Company and was recrystallized twice from n-hexane prior to use. 3-Aminopyridine adenine dinucleotide was prepared chemically from NAD as described by Fisher et al (1973). After purification by ion-exchange chromatography on Dowex-l-formate, the dinucleotide was desalted by gel filtration on a Sephadex 0021-8561/78/1426-0134$01.00/0 © 1978 American Chemical Society G-10 column.…”

Section: Methodsmentioning

confidence: 99%

“…The first experiment involved the quenching of fluorescence of the pyridine nucleotide coenzyme analogue, 3-aminopyridine adenine dinucleotide. This compound which contains a fluorescing pyridinium base has been shown to be very sensitive to charge-transfer complex formation with halogens resulting in the quenching of fluorescence of the 3-aminopyridine moiety (Fisher et al, 1973). A 5 X 10~4 solution of 3-aminopyridine adenine dinucleotide in 50 mM Tris-HCl buffer, pH 8.1, and 10% ethanol was excited at 331 nm and the fluorescence at 420 nm was recorded.…”

Section: Minutesmentioning

confidence: 99%

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Interactions of Kepone with rabbit muscle lactate dehydrogenase

Anderson¹,

Kohler²,

Young³

1978

J. Agric. Food Chem.

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“…three halogenated coenzyme analogues show coenzyme activity with LADH.29, [34][35][36] The binding to LADH in the crystalline state of I3PdAD+ 6 and PdAD+ 3 was determined under such conditions that crystals of the complexes are isomorphous with apoenzyme crystals. The results were quite unexpected.…”

Section: Dinucleotidementioning

confidence: 99%

Chemistry and structure of alcohol dehydrogenase: some general considerations on binding mode variability

Biellmann¹

1986

Acc. Chem. Res.

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Interactions of 3-Aminopyridine Adenine Dinucleotide with Dehydrogenases

Cited by 66 publications

References 20 publications

Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (Il84Y) in the pyridine nucleotide binding domain

Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (Il84Y) in the pyridine nucleotide binding domain

Interactions of Kepone with rabbit muscle lactate dehydrogenase

Chemistry and structure of alcohol dehydrogenase: some general considerations on binding mode variability

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