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Appl. Environ. Microbiol., Dec 1997, 4839-4843, Vol 63, No. 12
Z He and JC Spain
Pseudomonas pseudoalcaligenes JS45 utilizes nitrobenzene as the sole source
of nitrogen, carbon, and energy. Previous studies have shown that
degradation of nitrobenzene involves the reduction of nitrobenzene to
nitrosobenzene and hydroxylaminobenzene, followed by rearrangement to
2-aminophenol, which then undergoes meta ring cleavage to 2- aminomuconic
semialdehyde. In the present paper, we report the enzymatic reactions
responsible for the release of ammonia after ring cleavage. 2-Aminomuconic
semialdehyde was oxidized to 2-aminomuconate in the presence of NAD by
enzymes in crude extracts. 2-Aminomuconate was subsequently deaminated
stoichiometrically to 4-oxalocrotonic acid. No cofactors are required for
the deamination. Two enzymes, 2- aminomuconic semialdehyde dehydrogenase
and a novel 2-aminomuconate deaminase, distinguished by partial
purification of the crude extracts, catalyzed the two reactions.
4-Oxalocrotonic acid was further degraded to pyruvate and acetaldehyde. The
key enzyme, 2-aminomuconate deaminase, catalyzed the hydrolytic deamination
that released ammonia, which served as the nitrogen source for growth of
the organism.
Copyright © 1997, American Society for Microbiology
Studies of the catabolic pathway of degradation of nitrobenzene by Pseudomonas pseudoalcaligenes JS45: removal of the amino group from 2- aminomuconic semialdehyde
Air Force Research Laboratory, Tyndall Air Force Base, Floride 32403, USA. jspain@ccmail.aleq.tyndall.af.mil
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