2-Hydroxyisonicotinate dehydrogenase isolated from Mycobacterium sp. INA1.

Abstract:

:2-Hydroxyisonicotinate dehydrogenase from Mycobacterium sp. INA1 was purified 26-fold to apparent homogeneity. The enzyme is involved in isonicotinate degradation by Mycobacterium sp. INA1 and catalyzes the conversion of 2-hydroxyisonicotinate to 2,6-dihydroxypyridine-4-carboxylate. The purified protein exhibited a native molecular mass of 300 kDa and subunits of 97, 31 and 17 kDa, respectively, indicating an alpha 2 beta 2 gamma 2 structure. The absorption spectrum of the homogeneous enzyme was characteristic for an iron/sulfur flavoprotein, 3.8 mol of iron, 3.7 mol of acid labile sulfur, 0.94 mol of FAD and 0.75 mol of molybdenum were determined per mol of protomer. The molybdenum cofactor was identified as molybdopterin cytosine dinucleotide. 2-Hydroxyisonicotinate dehydrogenase was inactivated in the presence of cyanide. According to these basic properties the protein seems to belong to the class of molybdo-iron/sulfur flavoproteins of the xanthine oxidase family.

journal_name

FEMS Microbiol Lett

authors

Schräder T,Hillebrand C,Andreesen JR

doi

10.1111/j.1574-6968.1998.tb13103.x

subject

Has Abstract

pub_date

1998-07-15 00:00:00

pages

311-6

issue

2

eissn

0378-1097

issn

1574-6968

pii

S0378-1097(98)00232-8

journal_volume

164

pub_type

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