Results 91 to 100 of about 3,470 (203)
Xin Liu,1 Lili An,2 Shuaijun Ren,2 Yonghui Zhou,1 Wei Peng1 1College of Basic Medicine, Guizhou University of Traditional Chinese Medicine, Guiyang, Guizhou, 550025, People’s Republic of China; 2Dermatology Department, The First Affiliated Hospital of ...
Liu X, An L, Ren S, Zhou Y, Peng W
doaj
The carbamoyltransferase or aspartate carbamoyltransferase (ATCase)/ornithine carbamoyltransferase (OTCase) is an evolutionary conserved protein family, which contains two genes, ATCase and OTCase. The ATCase catalyzes the committed step in the synthesis
Yogeshwar V. Dhar (14049000) +1 more
core +1 more source
Two different approaches provided evidence for a physical interaction between the carbamate kinase-like carbamoyl-phosphate synthetase (CKase) and ornithine carbamoyltransferase (OTCase) from the hyperthermophilic archaeon Pyrococcus furiosus.
Legrain, Christiane +9 more
core +1 more source
Branched-chain amino acids (BCAAs) are important for normal growth, development, and function. In urea cycle disorders (UCDs), plasma BCAA levels can be relatively low; this has been attributed variously to low protein intake, hyperammonaemia, and ...
Mildrid Yeo +4 more
doaj +1 more source
In Agrobacterium tumefaciens and Rhizobia arginine can be used as the sole nitrogenous nutrient via degradation by an inducible arginase. These microorganisms were found to exhibit arginine inhibition of ornithine carbamoyltransferase activity.
Legrain, Christiane +2 more
core
The catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa, an enzyme consisting of 12 identical 38-kDa subunits, displays allosteric properties, namely carbamoylphosphate homotropic cooperativity and heterotropic activation by AMP and ...
Petillot, Yves +5 more
core +1 more source
Ornithine Carbamoyltransferase from Spinacea oleracea: Purification and Characterization
Ornithine carbamoyltransferase (OCT) from spinach (Spinacea oleracea L.) was purified to homogeneity and studied for some kinetic and structural properties. The enzyme showed a specific activity of 436 U mg−1, its molecular mass was approximately 118 kDa as estimated by Sephacryl S-200 gel filtration chromatography, the purified protein ran as a single
BELLOCCO, Ersilia Santa +6 more
openaire +3 more sources
Ornithine carbamoyltransferase from E. coli W was purified to homogeneity. The enzyme has a molecular weight of 105000. It is composed of three apparently identical subunits with molecular weights of 35000.
Legrain, Christiane, Stalon, Victor
core
Listeria monocytogenes (L. monocytogenes) is a major foodborne pathogen which can invade intestinal epithelial cells and cause severe systemic infection.
Yao He +6 more
doaj +1 more source
Linker insertion mutagenesis based on IS21 transposition: isolation of an AMP-insensitive variant of catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa [PDF]
The bacterial insertion sequence IS21 when repeated in tandem efficiently promotes non-replicative cointegrate formation in Escherichia coli. An IS21-IS21 junction region which had been engineered to contain unique SalI and BglII sites close to the IS21 ...
Berger, Bernard +7 more
core

