Enzymes involved in anaerobic degradation of acetone by a denitrifying bacterium.

Abstract:

:The pathway of anaerobic acetone degradation by the denitrifying bacterial strain BunN was studied by enzyme measurements in extracts of anaerobic acetone-grown cells. An ADP- and MgCl2-dependent decarboxylation of acetoacetate was detected which could not be found in cell-free extracts of acetate-grown cells. It is concluded that free acetoacetate is formed by ATP-dependent carboxylation of acetone. Acetoacetate was converted into its coenzyme A ester by succinyl-CoA: acetoacetate CoA transferase, and cleaved by a thiolase into acetyl-CoA. The acetyl residue was completely oxidized in the citric acid cycle. The ADP-dependent decarboxylation of acetoacetate was inhibited by EDTA, but not by avidin. High myokinase activities led to equilibrium amounts of ATP, ADP, and AMP in the reaction mixtures, and prevented determination of the decarboxylase reaction stoichiometry, therefore.

journal_name

Biodegradation

journal_title

Biodegradation

authors

Platen H,Schink B

doi

10.1007/BF00119761

subject

Has Abstract

pub_date

1990-01-01 00:00:00

pages

243-51

issue

4

eissn

0923-9820

issn

1572-9729

journal_volume

1

pub_type

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