J. Biol. Chem., Vol. 262, Issue 19, 8994-9003, 07, 1987
Enzymatic reactions in the degradation of 5-aminovalerate by Clostridium aminovalericum
HA Barker, L D'Ari and J Kahn
The anaerobic degradation of 5-aminovalerate to valerate, acetate,
propionate, and ammonia by Clostridium aminovalericum was shown to involve
the following intermediates: glutaric semialdehyde, 5- hydroxyvalerate,
5-hydroxyvaleryl-CoA, 4-pentenoyl-CoA, 2,4- pentadienoyl-CoA,
trans-2-pentenoyl-CoA, L-3-hydroxyvaleryl-CoA, 3- ketovaleryl-CoA, acetyl-
and propionyl-CoA and the corresponding acylphosphates, valeryl-CoA, and
possibly 3-pentenoyl-CoA. With exception of the enzyme presumably reducing
2,4-pentadienoyl-CoA to 3- pentenoyl-CoA, enzymes catalyzing the formation
and utilization of the above intermediates were demonstrated in extracts.
Trans-2-pentenoyl- CoA was shown to be the immediate precursor of
valeryl-CoA. The reduction of 2-pentenoyl-CoA was found to be coupled to
the oxidation of 4-pentenoyl-CoA to 2,4-pentadienoyl-CoA. Several enzymes
catalyzing the above reactions were partially purified and some of their
properties determined. A high pressure liquid chromatography method of
identifying and estimating most of the above mentioned CoA thiolesters was
developed.
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