[2] NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas

Autor:	Hansen, TA, Hensgens, CMH, Peck, Jr., Harry D., LeGall, Jean
Jazyk:	angličtina
Rok vydání:	1994
Předmět:	chemistry.chemical_classification Ethanol biology Stereochemistry biology.organism_classification Desulfovibrio Propanol chemistry.chemical_compound Enzyme chemistry Biochemistry biology.protein Glycerol Desulfovibrio gigas NAD+ kinase Alcohol dehydrogenase
Zdroj:	Inorganic Microbial Sulfur Metabolism, 17-21 STARTPAGE=17;ENDPAGE=21;TITLE=Inorganic Microbial Sulfur Metabolism
DOI:	10.1016/0076-6879(94)43004-7
Popis:	Publisher Summary This chapter describes assay, purification, and properties of alcohol dehydrogenase from Desulfovibrio gigas. Desulfovibrio gigas NCIB 9332 and several other Desulfovibrio strains employ an NAD-dependent alcohol dehydrogenase for the dehydrogenation of short primary alcohols (especially ethanol and propanol) to the corresponding aldehydes. Alcohol dehydrogenase can be assayed by measurement of the change in absorbance at 340 nm as a result of the formation or disappearance of NADH. In view of the oxygen lability of the enzyme, the assays are preferably carried out under N 2 although with sufficiently active preparations acceptable results can be obtained in aerobic assays. One unit is defined as the amount of enzyme that catalyzes the reduction of 1 μ mol of NAD + per minute. The purified enzyme is rapidly inactivated by exposure to air. The enzyme is strongly inhibited by 2 m M N -ethylmaleimide, 2 m M Cu 2+ , and 0.04 m M Zn 2+ . The enzyme rapidly catalyzes the oxidation of ethanol and propanol, is less active toward 1-butanol, 1,3-propanediol, 1,2-propanediol, and glycerol.
Databáze:	OpenAIRE
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