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B6db references: 4407783

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
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

B6db references