|
type |
Journal Article |
authors |
Barker, H. A.; D'Ari, L.; Kahn, J. |
title |
Enzymatic reactions in the degradation of 5-aminovalerate by Clostridium aminovalericum |
journal |
J Biol Chem |
Activity |
2.6.1.48 |
ui |
87250536 |
year |
(1987) |
volume |
262 |
number |
19 |
pages |
8994-9003. |
| |
keywords |
Amino Acids/*metabolism |
abstract |
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. |
last changed |
2002/11/12 16:17 |
|