Glutamine amidotransferase

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.

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

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
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.