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J. Biol. Chem., Vol. 268, Issue 29, 21466-21469, 10, 1993

A bacterial enzyme that catalyzes formation of carbon monoxide

JW Wray and RH Abeles
Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254.

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.
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