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Glutamine amidotransferase

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Glutamine amidotransferase class-I
crystal structure of putative glutamine amido transferase (tm1158) from thermotoga maritima at 1.70 a resolution
Identifiers
SymbolGATase
PfamPF00117
Pfam clanCL0014
InterProIPR000991
PROSITEPDOC00406
MEROPSC44
SCOP21ea0 / SCOPe / SUPFAM
CDDcd01653
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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.

References

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  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