urea carboxylase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 6.3.4.6 | ||||||||
CAS no. | 9058-98-4 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
|
In enzymology, a urea carboxylase (EC 6.3.4.6) is an enzyme that catalyzes the chemical reaction
The 3 substrates of this enzyme are ATP, urea, and HCO3-, whereas its 3 products are ADP, phosphate, and urea-1-carboxylate (allophanate).
This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is urea:carbon-dioxide ligase (ADP-forming). This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, biotin.
Carbamoyl phosphate synthetase I is a ligase enzyme located in the mitochondria involved in the production of urea. Carbamoyl phosphate synthetase I transfers an ammonia molecule to a molecule of bicarbonate that has been phosphorylated by a molecule of ATP. The resulting carbamate is then phosphorylated with another molecule of ATP. The resulting molecule of carbamoyl phosphate leaves the enzyme.
The long chain fatty acyl-CoA ligase is an enzyme of the ligase family that activates the oxidation of complex fatty acids. Long chain fatty acyl-CoA synthetase catalyzes the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. The enzyme catalyzes the following reaction,
Phosphoribosylformylglycinamidine cyclo-ligase is the fifth enzyme in the de novo synthesis of purine nucleotides. It catalyzes the reaction to form 5-aminoimidazole ribotide (AIR) from formylglycinamidine-ribonucleotide FGAM. This reaction closes the ring and produces a 5-membered imidazole ring of the purine nucleus (AIR):
In enzymology, a 2-oxoglutarate carboxylase (EC 6.4.1.7) is an enzyme that catalyzes the chemical reaction
Carnosine synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a D-alanine—D-alanine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a dihydrofolate synthase is an enzyme that catalyzes the chemical reaction
In enzymology, a formate—tetrahydrofolate ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a glutamate-putrescine ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a glutathionylspermidine synthase is an enzyme that catalyzes the chemical reaction
In enzymology, an isoleucine—tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a phosphopantothenate—cysteine ligase also known as phosphopantothenoylcysteine synthetase (PPCS) is an enzyme that catalyzes the chemical reaction which constitutes the second of five steps involved in the conversion of pantothenate to Coenzyme A. The reaction is:
In molecular biology, the protein domain SAICAR synthase is an enzyme which catalyses a reaction to create SAICAR. In enzymology, this enzyme is also known as phosphoribosylaminoimidazolesuccinocarboxamide synthase. It is an enzyme that catalyzes the chemical reaction
In enzymology, a phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a succinate-CoA ligase (ADP-forming) is an enzyme that catalyzes the chemical reaction
In enzymology, a tetrahydrofolate synthase is an enzyme that catalyzes the chemical reaction
In enzymology, an allophanate hydrolase (EC 3.5.1.54) is an enzyme that catalyzes the chemical reaction
In enzymology, a myosin-heavy-chain kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a xylulokinase is an enzyme that catalyzes the chemical reaction
Daniel Edward Atkinson was an American biochemist who worked at UCLA for 40 years from 1952 until his retirement in 1992, though he continued his scientific work as Emeritus Professor. He is best known for the concept of energy charge.