Glutamine amidotransferase: Difference between revisions
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In molecular biology, '''glutamine amidotransferases''' (GATase) are [[enzymes]] which [[catalyse]] the removal of the [[ammonia]] group from a [[ |
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 [[Enzyme substrate|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) [[protein domain|domains]] can occur either as single polypeptides, as in glutamine amidotransferases, or as [[protein domains|domains]] in a much larger multifunctional [[synthase]] protein, such as CPSase. On the basis of [[sequence (biology)|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)<ref name="pmid3298209">{{cite journal | author = Weng ML, Zalkin H | title = Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain | journal = J. Bacteriol. | volume = 169 | issue = 7 | pages = 3023–8 | year = 1987 | month = July | pmid = 3298209 | pmc = 212343 | doi = | url = }}</ref><ref name="pmid6086650">{{cite journal | author = Nyunoya H, Lusty CJ | title = Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain | journal = J. Biol. Chem. | volume = 259 | issue = 15 | pages = 9790–8 | year = 1984 | month = August | pmid = 6086650 | doi = | url = }}</ref>. Class-I GATase domains are defined by a [[conserved sequence|conserved]] [[catalytic triad]] consisting of [[cysteine]], [[histidine]] and [[glutamate]]. Class-I GPTase 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. |
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==References== |
==References== |
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Revision as of 04:16, 9 May 2012
| Glutamine amidotransferase class-I | |||||||||
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 crystal structure of putative glutamine amido transferase (tm1158) from thermotoga maritima at 1.70 a resolution | |||||||||
| Identifiers | |||||||||
| Symbol | GATase | ||||||||
| Pfam | PF00117 | ||||||||
| Pfam clan | CL0014 | ||||||||
| InterPro | IPR000991 | ||||||||
| PROSITE | PDOC00406 | ||||||||
| MEROPS | C44 | ||||||||
| SCOP2 | 1ea0 / SCOPe / SUPFAM | ||||||||
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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 GPTase 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
- ^ Weng ML, Zalkin H (1987). "Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain". J. Bacteriol. 169 (7): 3023–8. PMC 212343. PMID 3298209.
{{cite journal}}: Unknown parameter|month=ignored (help) - ^ Nyunoya H, Lusty CJ (1984). "Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain". J. Biol. Chem. 259 (15): 9790–8. PMID 6086650.
{{cite journal}}: Unknown parameter|month=ignored (help)