type	Journal Article
authors	Tsai, C.H. and Henderson, L.M.
title	Degradation of O-phosphohydroxylysine by rat liver. Purification of the phospho-lyase.
journal	J. Biol. Chem.
Activity	4.2.3.134
sel	selected
ui	4412716
year	(1974)
volume	249
pages	5784-5789
abstract	The first of two enzymes involved in the conversion of O- phosphohydroxylysine to 2-aminoadipate, has been purified ZSO-fold from rat liver. The product of this phospho-lyase is 2-aminoadipate semialdehyde and both phosphohydroxy-L- lysine and phosphoallohydroxy-L-fysine are substrates with K,,, values of 3.6 PM and 10.5 PM, respectively. The enzyme is dependent upon pyridoxal phosphate, which can be removed by dialysis against a phosphate-O.1 M cysteine buBer. The resulting apoenzyme had a residual activity of less than 1% that of the holoenzyme, and full activity was restored within 10 min by incubation with 10 PM pyridoxal phosphate; the co- enzyme was inhibitory at higher concentrations. Treatment with borohydride inactivated the holoenzyme, but had no ef- fect on the apoenzyme. The apparent K,,, for pyridoxal phosphate was 3.8 PM. ‘I he molecular weight was estimated to be 140,000 by Sephadex G-150 gel filtration.
last changed	2016/09/30 16:22