type	Journal Article
authors	Cooper, A. J.; Meister, A.
title	Enzymatic conversion of O-carbamyl-L-serine to pyruvate and ammonia
journal	Biochem Biophys Res Commun
Activity	4.3.1.13
sel	selected
ui	4761084
year	(1973)
volume	55
number	3
pages	780-7
keywords	Alanine Transaminase/metabolism
abstract	O-Carbamyl-L-serine is converted to pyruvate and ammonia by rat liver homogenates. This enzymatic activity was purified about 90-fold; it is distinct from glutamate-aspartate, glutamate-alanine, and soluble glutamine transaminases, and from O-sulfo-L-serine deaminase. The purified preparation catalyzed the formation of 2 moles of NH3 per mole of pyruvate formed. The preparation did not act on the L- or DL-forms of threonine, serine, homoserine, cysteine and O-phosphoserine, or L-alanine. Purified rat liver glutamine transaminases L and K and commercially available pig heart glutamate-aspartate and glutamate-alanine transaminases deaminated O-carbamyl L-serine very slowly. β-Chloro-L-alanine irreversibly inactivated glutamine transaminases L and K and the purified O-carbamyl-L-serine deaminase preparation.
last changed	2009/06/26 15:45