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B6db references: 4761084

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
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

B6db references