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J. Biol. Chem., Vol. 268, Issue 29, 21466-21469, 10, 1993
JW Wray and RH Abeles
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.
A bacterial enzyme that catalyzes formation of carbon monoxide
Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254.
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