Results 151 to 160 of about 3,470 (203)

The specialization of the two ornithine carbamoyltransferases of Pseudomonas

open access: yesBiochimica et Biophysica Acta (BBA) - Enzymology, 1967
Abstract The two ornithine carbamoyltransferases (carbamoylphosphate: l -ornithine carbamoyltransferase, EC 2.1.3.3) of Pseudomonas are integrated into different metabolic sequences. This integration appears both in their regulation and in their activities.
Ramos, Fernando   +3 more
openaire   +4 more sources

The occurrence of a catabolic and an anabolic ornithine carbamoyltransferase in Pseudomonas

open access: yesBiochimica et Biophysica Acta (BBA) - Enzymology, 1967
Abstract The occurrence of two ornithine carbamoyltransferases (carbamoylphosphate: l -ornithine carbamoyltransferase, EC 2.1.3.3) in Pseudomonas is demonstrated by their separation with ammonium sulfate. The two enzymes are distinguished by their activities as a function of pH. On the basis of the regulation of their synthesis, an anabolic function
Stalon, Victor   +3 more
openaire   +4 more sources

Kinetic studies of allosteric catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa

open access: yesFEBS Journal, 1998
The pseudo-reverse reaction of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase in which arsenate is first coupled to citrulline followed by elimination of carbamylarsenate has been studied.
Catherine Tricot   +2 more
exaly   +2 more sources

Refined structure ofPyrococcus furiosusornithine carbamoyltransferase at 1.87 A [PDF]

open access: yesActa Crystallographica Section D: Biological Crystallography, 2003
Using synchrotron radiation, X-ray data have been collected from Pyrococcus furiosus ornithine carbamoyltransferase (Pfu OTCase) to a maximal resolution of 1.87 Å, allowing the refinement of a previous structure at 2.7 Å [Villeret et al.
Johan Wouters   +2 more
exaly   +2 more sources

Biochemical Characterisation of Ornithine Carbamoyltransferase from Pyrococcus Furiosus

open access: yesFEBS Journal, 1997
Ornithine carbamoyltransferase (OTCase) was purified to homogeneity from the hyperthermophilic archaeon Pyrococcus furiosus. The enzyme is a 400 ± 20-kDa polymer of a 35-kDa subunit, in keeping with the corresponding gene sequence [Roovers, M. Hethke, C.
Christianne Legrain   +2 more
exaly   +1 more source

Staphylococcal Ornithine Carbamoyltransferase

European Journal of Biochemistry, 1971
A procedure for the purification of an ornithine carbamoylphosphate transferase isolated from a Staphylococcus aureus strain is reported. The procedure consists of the following steps: water extraction of the crude enzyme by autolysis under a toluene layer of the acetone dried bacteria cells, lyophilization of the crude extract, molecular sieving ...
O, Zaharia, E, Soru
openaire   +2 more sources

Endosymbiont as supplier of ornithine carbamoyltransferase in a trypanosomatid

Nature, 1977
IN spite of the widespread occurrence of intracellular bacteria-like symbionts in eukaryotic cells little is known about their function1–3. They are generally thought to offer some advantage to the host cell while benefiting from its ‘hospitality’, but their precise contribution is known in few cases.
Camargo, E. P., Freymuller, E.
openaire   +3 more sources

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