GMP synthase
| GMP synthase | ||
|---|---|---|
|
||
| GMP synthase dimer from E. coli according to PDB 1GPM | ||
| Properties of human protein | ||
| Mass / length primary structure | 692 amino acids | |
| Secondary to quaternary structure | Homodimer | |
| Identifier | ||
| Gene name | GMPS | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 6.3.5.2 , ligase | |
| Substrate | ATP + XMP + glutamine + H 2 O | |
| Products | AMP + PP i + GMP + glutamate | |
| Occurrence | ||
| Parent taxon | Creature | |
| Orthologue | ||
| human | House mouse | |
| Entrez | 8833 | 229363 |
| Ensemble | ENSG00000163655 | ENSMUSG00000027823 |
| UniProt | P49915 | Q3THK7 |
| Refseq (mRNA) | NM_003875 | NM_001033300 |
| Refseq (protein) | NP_003866 | NP_001028472 |
| Gene locus | Chr 3: 155.87 - 155.94 Mb | Chr 3: 63.98 - 64.02 Mb |
| PubMed search | 8833 |
229363
|
The GMP synthase is the enzyme in all living beings, the last step in the de novo synthesis of GMP catalyzes : the conversion of Xanthosinmonophosphat (XMP). GMP is the precursor to both the nucleotide GTP , which acts as an energy carrier like ATP, and the purine base guanosine , which is indispensable in the genome .
The reaction takes place in two steps: after cleavage of Polyphosphatrests of ATP following hydrolysis of glutamine with transfer of the amino group . Both individual reactions are catalyzed by their own domain , both of which are located on the enzyme. Only some archaea have a single enzyme for each domain.
Catalyzed reaction
+ 
+ ATP + H 2 O + + AMP + PP i
GMP, AMP and glutamic acid are created from XMP, ATP and glutamine.
literature
- M. Hirst, E. Haliday, et al. a .: Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. In: The Journal of biological chemistry. Volume 269, No. 38, September 1994, pp. 23830-23837. PMID 8089153 .
Individual evidence
Web links
Wikibooks: Biochemistry and Pathobiochemistry: Purine Metabolism - Learning and Teaching Materials
