|
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 |
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