|
type |
Journal Article |
authors |
Jeng IM, Somack R, Barker HA. |
title |
Ornithine degradation in Clostridium sticklandii; pyridoxal phosphate and coenzyme A dependent thiolytic cleavage of 2-amino-4-ketopentanoate to alanine and acetyl coenzyme A. |
journal |
Biochemistry |
Activity |
2.3.1.263 |
sel |
selected |
ui |
4407783 |
year |
(1974) |
volume |
13 |
number |
14 |
pages |
2898-903 |
| |
keywords |
Amines |
abstract |
The third enzymic step in the fermentation Of D-Ornithine by Clostridium Sticklandii was identified as a thioly-tic cleavage of 2-amino-4-ketopentanoate By coenzyme A To form acetyl-CoA and alanine. Satisfactory Radiochemical and spectrophotometric assays were developed for the 2-amino-4-Ketopentanoate thiolase catalyzing this reaction. The Activity of this partially purified thiolase is completely dependent on the presence of pyridoxal 5'-phosphate. The Apparent Km for this coenzyme is 2.5X10-7M.The Enzyme is completely inactivated by dialysis against 100mM cysteine and can be reacti-vated by the addition of pyridoxal S'-phosphate.Other Pyridoxal phosphate analogs and ketoacids cannot replace pyridoxal 5'-phosphate. The structure of 2-amino-4-ketopentanoate was verified by several chromatographic and electrophoretic procedures and by identification of the products of iodoform degradation. |
last changed |
2018/02/14 11:12 |
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