Glutamine amidotransferase

Last updated
Glutamine amidotransferase class-I
PDB 1o1y EBI.jpg
crystal structure of putative glutamine amido transferase (tm1158) from thermotoga maritima at 1.70 a resolution
Identifiers
SymbolGATase
Pfam PF00117
Pfam clan CL0014
InterPro IPR000991
PROSITE PDOC00406
MEROPS C44
SCOPe 1ea0 / SUPFAM
CDD cd01653

In molecular biology, glutamine amidotransferases (GATase) are enzymes which catalyse the removal of the ammonia group from a glutamine molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This activity is found in a range of biosynthetic enzymes, including glutamine amidotransferase, anthranilate synthase component II, p-aminobenzoate, and glutamine-dependent carbamoyl-transferase (CPSase). Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. On the basis of sequence similarities two classes of GATase domains have been identified: class-I (also known as trpG-type) and class-II (also known as purF-type). [1] [2] Class-I GATase domains are defined by a conserved catalytic triad consisting of cysteine, histidine and glutamate. Class-I GATase domains have been found in the following enzymes: the second component of anthranilate synthase and 4-amino-4-deoxychorismate (ADC) synthase; CTP synthase; GMP synthase; glutamine-dependent carbamoyl-phosphate synthase; phosphoribosylformylglycinamidine synthase II; and the histidine amidotransferase hisH.

Related Research Articles

Aspartate carbamoyltransferase Protein family

Aspartate carbamoyltransferase catalyzes the first step in the pyrimidine biosynthetic pathway.

Biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined together to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.

Glutamine synthetase class of enzymes

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 from glutamine or glutamate 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.

Amino acid synthesis biological synthesis of amino acids

Amino acid synthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can only synthesize 11 of the 20 standard amino acids, and in time of accelerated growth, histidine can be considered an essential amino acid.

CAD protein protein-coding gene in the species Homo sapiens

CAD protein is a trifunctional multi-domain enzyme involved in the first three steps of pyrimidine biosynthesis. De-novo synthesis starts with cytosolic carbamoylphosphate synthetase II which uses glutamine, carbon dioxide and ATP. This enzyme is inhibited by uridine triphosphate.

CTP synthetase InterPro Family

CTP synthase is an enzyme involved in pyrimidine biosynthesis that interconverts UTP and CTP.

Carbamoyl phosphate synthetase class of enzymes

Carbamoyl phosphate synthetase catalyzes the ATP-dependent synthesis of carbamoyl phosphate from glutamine or ammonia and bicarbonate. This enzyme catalyzes the reaction of ATP and bicarbonate to produce carboxy phosphate and ADP. Carboxy phosphate reacts with ammonia to give carbamic acid. In turn, carbamic acid reacts with a second ATP to give carbamoyl phosphate plus ADP.

Carbamoyl phosphate synthetase II is an enzyme that catalyzes the reactions that produce carbamoyl phosphate in the cytosol. Its systemic name is hydrogen-carbonate:L-glutamine amido-ligase .

GMP synthase mammalian protein found in Homo sapiens

Guanosine monophosphate synthetase, also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate.

Amidophosphoribosyltransferase mammalian protein found in Homo sapiens

Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme responsible for catalyzing the conversion of 5-phosphoribosyl-1-pyrophosphate (PRPP) into 5-phosphoribosyl-1-amine (PRA), using the amine group from a glutamine side-chain. This is the committing step in de novo purine synthesis. In humans it is encoded by the PPAT gene. ATase is a member of the purine/pyrimidine phosphoribosyltransferase family.

Ribose-phosphate diphosphokinase class of enzymes

Ribose-phosphate diphosphokinase is an enzyme that converts ribose 5-phosphate into phosphoribosyl pyrophosphate (PRPP). It is classified under EC 2.7.6.1.

Isopenicillin N synthase class of enzymes

Isopenicillin N synthase (IPNS) is a non-heme iron-dependent enzyme belonging to the oxidoreductase family. This enzyme catalyzes the formation of isopenicillin N from δ-(L-α-aminoadipoyl)-L-cysteinyl-D-valine (LLD-ACV).

Phosphoribosylanthranilate isomerase class of enzymes

In enzymology, a phosphoribosylanthranilate isomerase [ PRAI ] is an enzyme that catalyzes the third step of the synthesis of the amino acid tryptophan.

Anthranilate synthase class of enzymes

In enzymology, an anthranilate synthase is an enzyme that catalyzes the chemical reaction

Indole-3-glycerol-phosphate synthase class of enzymes

In enzymology, an indole-3-glycerol-phosphate synthase (IGPS) (EC 4.1.1.48) is an enzyme that catalyzes the chemical reaction

Aminodeoxychorismate synthase class of enzymes

In enzymology, an aminodeoxychorismate synthase is an enzyme that catalyzes the chemical reaction

In enzymology, a NAD+ synthase (glutamine-hydrolysing) (EC 6.3.5.1) is an enzyme that catalyzes the chemical reaction

Phosphoribosylformylglycinamidine synthase enzyme

In enzymology, a phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) is an enzyme that catalyzes the chemical reaction

Trypanothione synthase class of enzymes

In enzymology, a trypanothione synthase (EC 6.3.1.9) is an enzyme that catalyzes the chemical reaction

References

  1. Weng ML, Zalkin H (July 1987). "Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain". Journal of Bacteriology. 169 (7): 3023–8. doi:10.1128/jb.169.7.3023-3028.1987. PMC   212343 . PMID   3298209.
  2. Nyunoya H, Lusty CJ (August 1984). "Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain". The Journal of Biological Chemistry. 259 (15): 9790–8. PMID   6086650.
This article incorporates text from the public domain Pfam and InterPro: IPR000991