Work

Interactions of 3-Aminopyridine Adenine Dinucleotide with Dehydrogenases

Year: 1973

Type: article

Abstract: NAD was converted chemically to 3-aminopyridine adenine dinucleotide through the Hofmann hypobromite reaction and the resulting dinucleotide was purified by means of ion exchange chromatography. Spectrophotometric and fluorometric properties of the analog were studied. The 3-aminopyridine adenine dinucleotide was shown to be a competitive inhibitor in reactions catalyzed by seven NAD(P)-dependent enzymes. The 3-aminopyridine adenine dinucleotide was diazotized with the use of nitrous acid. The diazotized derivative was shown to be a site-specific inactivator of yeast alcohol dehydrogenase. Diazotized 3-amino-1-methylpyridinium chloride was prepared and shown to be less effective in the inactivation of this enzyme.

Source: Journal of Biological Chemistry

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

Authors: Tom L. Fisher, Sharon V. Vercellotti, Bruce M. Anderson

Institution: Virginia Tech

Language: English

Topic: Biochemical and Molecular Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1489176760

FWCI: 0.958

Cites: 22

Cited by: 65

Related to: 10