title: Primary structure, expression in Escherichia coli, and properties of S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase from Bacillus megaterium.
abstract: A Bacillus megaterium DNA fragment encoding S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase (SUMT) activity was subcloned and sequenced. The encoded polypeptide showed more than 43.5% strict homology to Pseudomonas denitrificans SUMT (F. Blanche, L. Debussche, D. Thibaut, J. Crouzet, and B. Cameron, J. Bacteriol. 171:4222-4231, 1989). The B. megaterium polypeptide was overexpressed in Escherichia coli, partially purified, and shown to exhibit, like P. denitrificans SUMT, substrate inhibition at uroporphyrinogen III concentrations above 0.5 microM, suggesting a common regulation for aerobic cobalamin-producing organisms.
authors.affiliation: Institut des Biotechnologies, Rhône-Poulenc Rorer S.A., Vitry sur Seine, France.
authors.forename: C
authors.initials: C
authors.lastname: Robin
authors.forename: F
authors.initials: F
authors.lastname: Blanche
authors.forename: L
authors.initials: L
authors.lastname: Cauchois
authors.forename: B
authors.initials: B
authors.lastname: Cameron
authors.forename: M
authors.initials: M
authors.lastname: Couder
authors.forename: J
authors.initials: J
authors.lastname: Crouzet
mesh_terms: D000595:Amino Acid Sequence; D001410:Bacillus megaterium / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005798:Genes, Bacterial; D008780:Methyltransferases / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D010957:Plasmids
chemical_list: D008780:Methyltransferases; C060508:uroporphyrin-III C-methyltransferase