[protein-PII] uridylyltransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.7.59 | ||||||||
CAS no. | 57657-57-5 | ||||||||
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 | ||||||||
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In enzymology, a [protein-PII] uridylyltransferase (EC 2.7.7.59) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are UTP and protein-PII, whereas its two products are diphosphate and [[uridylyl-[protein-PII]]].
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:[protein-PII] uridylyltransferase. Other names in common use include PII uridylyl-transferase, and uridyl removing enzyme. This enzyme participates in two-component system - general.
Glutamine synthetase (GS) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine:
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.
CTP synthase is an enzyme involved in pyrimidine biosynthesis that interconverts UTP and CTP.
UTP—glucose-1-phosphate uridylyltransferase also known as glucose-1-phosphate uridylyltransferase is an enzyme involved in carbohydrate metabolism. It synthesizes UDP-glucose from glucose-1-phosphate and UTP; i.e.,
Guanosine monophosphate synthetase, also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate.
In molecular biology, adenylosuccinate synthase is an enzyme that plays an important role in purine biosynthesis, by catalysing the guanosine triphosphate (GTP)-dependent conversion of inosine monophosphate (IMP) and aspartic acid to guanosine diphosphate (GDP), phosphate and N(6)-(1,2-dicarboxyethyl)-AMP. Adenylosuccinate synthetase has been characterised from various sources ranging from Escherichia coli to vertebrate tissues. In vertebrates, two isozymes are present: one involved in purine biosynthesis and the other in the purine nucleotide cycle.
The enzyme anthranilate synthase catalyzes the chemical reaction
The enzyme indole-3-glycerol-phosphate synthase (IGPS) (EC 4.1.1.48 ) catalyzes the chemical reaction
In enzymology, a glutamine—tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, an ATP phosphoribosyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a [glutamate—ammonia-ligase] adenylyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology and molecular biology, a holo-[acyl-carrier-protein] synthase is an enzyme that catalyzes the chemical reaction:
Phosphatidate cytidylyltransferase (CDS) is the enzyme that catalyzes the synthesis of CDP-diacylglycerol from cytidine triphosphate and phosphatidate.
In enzymology, an UDP-glucose—hexose-1-phosphate uridylyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an UDP-N-acetylglucosamine diphosphorylase is an enzyme that catalyzes the chemical reaction
In enzymology, an UTP—hexose-1-phosphate uridylyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an UTP—xylose-1-phosphate uridylyltransferase is an enzyme that catalyzes the chemical reaction
The PII family comprises a group of widely distributed signal transduction proteins found in nearly all Bacteria and also present in Archaea and in the chloroplasts of Algae and plants. PII form barrel-like homotrimers with a flexible loop, namely T-loop, emerging from each subunit. PII proteins have extraordinary sensory properties; they can exist in a vast range of structural status accordingly to the levels of ATP, ADP and 2-oxogluratate. These metabolites interact allosterically with PII in three conserved binding sites located in the lateral cavity between each PII subunit. ATP and ADP bind competitively to the nucleotide binding whereas the 2-oxoglutarate only interacts with PII in the presence of MgATP.
Asparagine synthase (glutamine-hydrolysing) (EC 6.3.5.4, asparagine synthetase (glutamine-hydrolysing), glutamine-dependent asparagine synthetase, asparagine synthetase B, AS, AS-B) is an enzyme with systematic name L-aspartate:L-glutamine amido-ligase (AMP-forming). This enzyme catalyses the following chemical reaction
The glnALG operon is an operon that regulates the nitrogen content of a cell. It codes for the structural gene glnA the two regulatory genes glnL and glnG. glnA encodes glutamine synthetase, an enzyme which catalyzes the conversion of glutamate and ammonia to glutamine, thereby controlling the nitrogen level in the cell. glnG encodes NRI which regulates the expression of the glnALG operon at three promoters, which are glnAp1, glnAp2 located upstream of glnA) and glnLp. glnL encodes NRII which regulates the activity of NRI. No significant homology is found in Eukaryotes.