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 Lettjournal_title
FEMS microbiology lettersauthors
Schräder T,Hillebrand C,Andreesen JRdoi
10.1111/j.1574-6968.1998.tb13103.xsubject
Has Abstractpub_date
1998-07-15 00:00:00pages
311-6issue
2eissn
0378-1097issn
1574-6968pii
S0378-1097(98)00232-8journal_volume
164pub_type
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