A bacterial enzyme that catalyzes formation of carbon monoxide.
We have isolated and purified an enzyme (E-2) from Klebsiella pneumoniae, which catalyzes the formation of CO from CH3-S-CH2-CH2-CO-C(OH) = CH-O- (III). This compound is an intermediate in the conversion of 5'-methylthioadenosine to methionine. Concomitant with CO formation, methylthiopropionic acid and formate are produced and O2 is consumed. E-2 also catalyzes the formation of CO, formate, and butyrate from CH3-CH2-CH2-CO-C(OH) = CH-O- (IIIa), the desthio analog of III. Experiments with isotopic IIIa have shown that formate is derived from 1-C, and CO from 2-C. E-2 has a M(r) = 18,500 and requires Mg2+, and no chromophoric cofactor has been detected.
Wray
J W
JW
Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254.
Abeles
R H
RH
D002248:Carbon Monoxide / Q000378:metabolism*; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D049308:Dioxygenases; D004591:Electrophoresis, Polyacrylamide Gel; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D010105:Oxygenases / Q000378:metabolism*; D013057:Spectrum Analysis
D002248:Carbon Monoxide; D010105:Oxygenases; D049308:Dioxygenases; C083734:aci-reductone oxidase (CO-forming)