[Purification and properties of 3-hexulosephosphate synthase from facultative methylotroph Pseudomonas oleovorans].
3-Hexulosephosphate synthase (HPS), the key enzyme of the hexulosephosphate cycle of formaldehyde fixation, was isolated from facultative methylotroph Pseudomonas oleovorans. Enzyme was purified 100-fold. The purification procedure involved fractionation with ammonium sulfate, gel-filtration on Sephadex G-150 and chromatography on DEAE-Sephadex A-50. The purified enzyme gave single band on analytical polyacrylamide gel electrophoresis. Optimal conditions for activity of HPS are: pH 7,0, temperature 50 degrees C. The molecular weight was calculated to be 45 000 from gel-filtration experiments. HPS is active only in the presence of Mg2+ or Mn2+. Ribulose-5-phosphate is the sole acceptor of formaldehyde. Activity of the enzyme is inhibited by NADH and NADPH.
D000446:Aldehyde-Lyases / Q000302:isolation & purification / Q000378:metabolism*; D006600:Hexosephosphates; D007700:Kinetics; D008697:Methane / Q000378:metabolism; D008970:Molecular Weight; D011549:Pseudomonas / Q000201:enzymology*; D012274:Ribulosephosphates
D006600:Hexosephosphates; D012274:Ribulosephosphates; D000446:Aldehyde-Lyases; C021355:hexose phosphate synthetase; D008697:Methane
Ochistka i kharakteristika 3-geksulozofosfatsintazy iz fakul'tativnogo metilotrofa Pseudomonas oleovorans.