Search results for "Carbamate kinase"

showing 2 items of 2 documents

Evolution of arginine deiminase (ADI) pathway genes

2002

We have analyzed the evolution of the three genes encoding structural enzymes of the arginine deiminase (ADI) pathway, arginine deiminase (ADI), ornithine transcarbamoylase (OTC), and carbamate kinase (CK) in a wide range of organisms, including Archaea, Bacteria, and Eukarya. This catabolic route was probably present in the last common ancestor to all the domains of life. The results obtained indicate that these genes have undergone a complex evolutionary history, including horizontal transfer events, duplications, and losses. Therefore, these genes are not adequate to infer organismal relationships at deep branching levels, but they provide an insight into how catabolic genes evolved and …

Most recent common ancestorHydrolasesMolecular Sequence DataBiologyModels BiologicalEvolution MolecularGeneticsAmino Acid SequenceMolecular BiologyArginine deiminase pathwayGeneArginine deiminaseOrnithine CarbamoyltransferasePhylogenyEcology Evolution Behavior and SystematicsGeneticsLikelihood FunctionsBacteriaSequence Homology Amino AcidPhylogenetic treeCarbamate kinaseFungiSequence Analysis DNAPhosphotransferases (Carboxyl Group Acceptor)ArchaeaMetabolic pathwayHorizontal gene transferMolecular Phylogenetics and Evolution
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Affinity Cleavage of Carbamoyl-Phosphate Synthetase I Localizes Regions of the Enzyme Interacting with the Molecule of ATP that Phosphorylates Carbam…

1995

Two ATP molecules are used in the reaction catalyzed by carbamoyl-phosphate synthetase I. One molecule (ATPA) phosphorylates HCO3- and the other (ATPB) phosphorylates carbamate. Carbamoyl-phosphate synthetase I is a 160-kDa polypeptide consisting of a 40-kDa N-terminal moiety and a 120-kDa C-terminal moiety, the latter being composed of two similar halves of molecular mass 60 kDa. We showed [Alonso, E., Cervera, J., Garcia-Espana, A., Bendala, E. & Rubio, V. (1992) J. Biol. Chem. 267, 4524-4532] that Fe.ATP bound at the site for ATPB catalyzes the oxidative inactivation of carbamoyl-phosphate synthetase I in a model oxidative system consisting of Fe3+, ascorbate, and O2, and we detected ATP…

chemistry.chemical_classificationbiologyChemistryProtein domainCarbamate kinaseCleavage (embryo)BiochemistryCarbamoyl phosphate synthetase IAmino acidBiochemistrybiology.proteinMoietyNucleotideBinding siteEuropean Journal of Biochemistry
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