peptidyl-glutaminase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.43 | ||||||||
CAS no. | 37228-70-9 | ||||||||
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 peptidyl-glutaminase (EC 3.5.1.43) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are alpha-N-peptidyl-L-glutamine and H2O, whereas its two products are alpha-N-peptidyl-L-glutamate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is peptidyl-L-glutamine amidohydrolase. Other names in common use include peptidoglutaminase I, peptideglutaminase, and peptidoglutaminase.
In organic chemistry, a peptide bond is an amide type of covalent chemical bond linking two consecutive alpha-amino acids from C1 of one alpha-amino acid and N2 of another, along a peptide or protein chain.
Guanosine monophosphate synthetase, also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate.
In enzymology, a NAD+ synthase (glutamine-hydrolysing) (EC 6.3.5.1) 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, an adenylyl-[glutamate---ammonia ligase] hydrolase (EC 3.1.4.15) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-(acetamidomethylene)succinate hydrolase (EC 3.5.1.29) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-(hydroxymethyl)-3-(acetamidomethylene)succinate hydrolase (EC 3.5.1.66) is an enzyme that catalyzes the chemical reaction
In enzymology, a 4-methyleneglutaminase (EC 3.5.1.67) is an enzyme that catalyzes the chemical reaction
In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide. In this way, the two substrates of this enzyme are an amide and H2O, whereas its two products are monocarboxylate and NH3.
In enzymology, a D-glutaminase (EC 3.5.1.35) is an enzyme that catalyzes the chemical reaction
In enzymology, a formimidoylglutamate deiminase (EC 3.5.3.13) is an enzyme that catalyzes the chemical reaction
In enzymology, a glutamin-(asparagin-)ase (EC 3.5.1.38) is an enzyme that catalyzes the chemical reaction
In enzymology, a N-formylglutamate deformylase (EC 3.5.1.68) is an enzyme that catalyzes the chemical reaction
In enzymology, an omega-amidase (EC 3.5.1.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a protein-arginine deiminase (EC 3.5.3.15) is an enzyme that catalyzes a form of post translational modification called arginine de-imination or citrullination:
In enzymology, a protein-glutamine glutaminase (EC 3.5.1.44) is an enzyme that catalyzes the chemical reaction
In enzymology, a theanine hydrolase (EC 3.5.1.65) is an enzyme that catalyzes the chemical reaction
In enzymology, a D-glutamyltransferase (EC 2.3.2.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a glutaminyl-peptide cyclotransferase (EC 2.3.2.5) is an enzyme that catalyzes the chemical reaction
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