FGAM synthase
| Phosphoribosylformylglycine amidine synthase | ||
|---|---|---|
| other names |
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| Properties of human protein | ||
| Mass / length primary structure | 1338 amino acids | |
| Identifier | ||
| Gene name | PFAS | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 6.3.5.3 , ligase | |
| Response type | Ketone Imine Conversion | |
| Substrate | FGAR + glutamine + ATP + H 2 O | |
| Products | FGAM + glutamate + ADP + P i | |
| Occurrence | ||
| Parent taxon | Creature | |
| Orthologue | ||
| human | House mouse | |
| Entrez | 5198 | 237823 |
| Ensemble | ENSG00000178921 | ENSMUSG00000020899 |
| UniProt | O15067 | Q5SUR0 |
| Refseq (mRNA) | NM_012393 | NM_001159519 |
| Refseq (protein) | NP_036525 | NP_001152991 |
| Gene locus | Chr 17: 8.25 - 8.27 Mb | Chr 11: 68.99 - 69.01 Mb |
| PubMed search | 5198 |
237823
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The FGAM synthase (FGAMS) (also FGARAT; formal: Phosphoribosylformylglycinamidin synthase) is the enzyme that in all living beings the fourth step of the purine biosynthesis catalyzes , namely the conversion of FGAR (a ketone ) to FGAM (an imine ). The FGAMS in most gram-negative bacteria and eukaryotes is a large protein that consists of three domains (N-terminal, FGAMS, glutaminase ), while in Gram-positive bacteria and archaea it is a complex of three individual proteins. The gene coding for the human enzyme was identified in 1999.
Catalyzed reaction
+ 
+ ATP + H 2 O + + ADP + P i
Phosphoribosylformylglycine amide (FGAR) and glutamine are converted to phosphoribosylformylglycine amidine (FGAM) and glutamic acid.
Individual evidence
- ↑ UniProt O15067
- ↑ M. Morar, AA Hoskins et al. a .: Formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima: structural insights into complex formation. In: Biochemistry. Volume 47, Number 30, July 2008, pp. 7816-7830, ISSN 1520-4995 . doi : 10.1021 / bi800329p . PMID 18597481 . PMC 2646663 (free full text).
- ↑ D. Patterson, J. Bleskan et al. a .: Human phosphoribosylformylglycineamide amidotransferase (FGARAT): regional mapping, complete coding sequence, isolation of a functional genomic clone, and DNA sequence analysis. In: Genes. Volume 239, Number 2, November 1999, pp. 381-391, ISSN 0378-1119 . PMID 10548741 .
Web links
Wikibooks: Purine Metabolism - Learning and Teaching Materials
