The Metabolism of Arginine in Serratia Marcescens II. Carbamy1-Adednosine Diphosphate Phosphoferase

Glasziou, KT

doi:10.1071/bi9560253

Cited by 10 publications

(2 citation statements)

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“…The present paper shows that this is not the case; CPSase from Serratia marcescens is very similar in regulatory properties to the well-characterized enzymes from E. coli and S. typhimurium and does not appear to be associated with other enzymes of pyrimidine biosynthesis. Carbamate kinase activity observed in crude extracts of S. marcescens is due to a constitutive acetate kinase (ATP:acetate phosphotransferase, EC 2.7.2.1) and not to a distinct carbamate kinase as was previously reported (9). Media and growth conditions.…”

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confidence: 60%

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Regulation of carbamylphosphate synthesis in Serratia marcescens

Crane¹,

Abdelal²

1980

J Bacteriol

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Serratia marcescens HY possessed a single carbamylphosphate synthase (CPSase) which was subject to cumulative repression by arginine and a pyrimidine. CPSase did not appear to be a part of a multifunctional enzyme complex as is the case for other enzymes of pyrimidine biosynthesis in this organism. CPSase was purified to homogeneity. The molecular weight of the enzyme was estimated to be 167,000 by sucrose density gradient ultracentrifugation. The double-reciprocal plot for magnesium adenosine triphosphate was linear, yielding a Km value of 2.5 mM. The enzyme utilized either glutamine (Km, 0.1 mM) or NH3 (Km, 10.5 mM) as a nitrogen donor in the reaction. CPSase activity was subject to activation by ornithine and feedback inhibition by uridine monophosphate, as is the case for other enteric bacteria. Carbamate kinase activity, detected in crude extracts of S. marcescens, was shown to be due to a constitutive acetate kinase. The absence of carbamate kinase from S. marcescens HY is consistent with the inability of this organism to utilize arginine as a source of energy under anaerobic conditions.

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confidence: 60%

“…Absence of a specific carbamate kinase from S. mcu-ce8cens. Glasziou reported the partial purification of a carbamate kinase from a strain of S. marcescens (9). Adequate criteria, however, were not used to distinguish between carbamate kinase activity and activities of acetate kinase and CPSase (for a review, see reference 1).…”

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confidence: 99%