Open AccessPurification, crystallization and preliminary X‐ray investigation of quinoprotein methylamine dehydrogenase from Thiobacillus versutu
Author(s) -
VELLIEUX Frederic M. D.,
FRANK Jzn Johannes,
SWARTE Myra B. A.,
GROENDIJK Hillie,
DUINE Johannis A.,
DRENTH Jan,
HOL Wim G. J.
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09409.x
Subject(s) - methylamine , isoelectric point , chemistry , oxidoreductase , ethylamine , electron acceptor , gel electrophoresis , enzyme , nuclear chemistry , chromatography , biochemistry , organic chemistry
The enzyme methylamine dehydrogenase or primary‐amine:(acceptor) oxidoreductase (deaminating) (EC 1.4.99.3) was purified from the bacterium Thiobacillus versutus to homogeneity, as judged by polyacrylamide gel electrophoresis. The native enzyme has a M r of 123 500 and contains four subunits arranged in a α 2 β 2 configuration, the light and heavy subunits having a M r of 12 900 and 47 500 respectively. The isoelectric point is 3.9. The purified enzyme was crystallized from 37–42% saturated ammonium sulphate in 0.1 M sodium acetate buffer, pH 5.0. The space group is P 3 1 21 or P 3 2 21, with one α 2 β 2 molecule in the asymmetric unit. The cell dimensions are: a = b = 13.01 nm; c = 10.40 nm. The X‐ray diffraction pattern extends to at least 0.25‐nm resolution.