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