-transparent.png){kind=logo}
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 Mr of 123 500 and contains four subunits arranged in a alpha 2 beta 2 configuration, the light and heavy subunits having a Mr of 12900 and 47500 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 P3(1)21 or P3(2)21, with one alpha 2 beta 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.
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
December 1990,
Acta crystallographica. Section B, Structural science,
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
October 1993,
FEBS letters,
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
February 1988,
Journal of molecular biology,
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
November 1989,
FEBS letters,
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
April 1983,
Journal of molecular biology,
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
October 1995,
Biochemistry,
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
October 1988,
Journal of molecular biology,
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
September 1992,
Journal of molecular biology,
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
February 2008,
Acta crystallographica. Section F, Structural biology and crystallization communications,
F M Vellieux, and
J Frank, and
M B Swarte, and
H Groendijk, and
J A Duine, and
J Drenth, and
W G Hol
September 2008,
Acta crystallographica. Section F, Structural biology and crystallization communications,
