Adenylosuccinate Synthetase
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Adenylosuccinate Synthetase (AdSS) is part of the ligase family of enzymes. Its systematic name is IMP:L-aspartate ligase. It is mainly involved in purine bio-synthesis. It does this by catalyzing the GTP dependent changeover of IMP and aspartic acid to AMP. <ref>PMID:1698173 </ref> In Humans, AdSS catalyzes the first committed step in the purine nucleotide cycle by the de novo synthesis of adenosine monophosphate.<ref>PMID:649264</ref> | Adenylosuccinate Synthetase (AdSS) is part of the ligase family of enzymes. Its systematic name is IMP:L-aspartate ligase. It is mainly involved in purine bio-synthesis. It does this by catalyzing the GTP dependent changeover of IMP and aspartic acid to AMP. <ref>PMID:1698173 </ref> In Humans, AdSS catalyzes the first committed step in the purine nucleotide cycle by the de novo synthesis of adenosine monophosphate.<ref>PMID:649264</ref> | ||
| - | AdSS was isolated from Yersinia pestis CO92 and can be found in a variety of organisms ranging from yeast to bacteria to humans. | + | AdSS(3hid) was isolated from Yersinia pestis CO92 and can be found in a variety of organisms ranging from yeast to bacteria to humans. |
==Structure== | ==Structure== | ||
Revision as of 04:46, 28 March 2010
Adenylosuccinate Synthetase
Contents |
Introduction
Adenylosuccinate Synthetase (AdSS) is part of the ligase family of enzymes. Its systematic name is IMP:L-aspartate ligase. It is mainly involved in purine bio-synthesis. It does this by catalyzing the GTP dependent changeover of IMP and aspartic acid to AMP. [1] In Humans, AdSS catalyzes the first committed step in the purine nucleotide cycle by the de novo synthesis of adenosine monophosphate.[2]
AdSS(3hid) was isolated from Yersinia pestis CO92 and can be found in a variety of organisms ranging from yeast to bacteria to humans.
Structure
The AdSS enzyme is a dimer consisting of two identical monomeric subunits. The main structural component of each monomer is a centrally located beta sheet that is comprised of 10 strands. Nine of the 10 strands are parallel while the 10th strand is anti-parallel with respect to the other 9 strands. There are also several other secondary structures including 2 small 3/10 helices, two anti-parallel sheets consisting of 2 and 3 strands respectively. Additionally there are 11 alpha helices.[3]
Helices are highlighted in green and beta sheets are shown in orange .
Reaction Mechanism
AdSS undergoes the following amination reaction:
GTP + IMP + L-Asp -> GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP[4]
References
- ↑ Mukhopadhyay RP, Chandra AL. Keratinase of a streptomycete. Indian J Exp Biol. 1990 Jun;28(6):575-7. PMID:1698173
- ↑ Pierloot RA. The treatment of psychosomatic disorders by the general practitioner. Int J Psychiatry Med. 1977-1978;8(1):43-51. PMID:649264
- ↑ Poland BW, Silva MM, Serra MA, Cho Y, Kim KH, Harris EM, Honzatko RB. Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains. J Biol Chem. 1993 Dec 5;268(34):25334-42. PMID:8244965
- ↑ Van der Weyden MB, Kelly WN. Human adenylosuccinate synthetase. Partial purification, kinetic and regulatory properties of the enzyme from placenta. J Biol Chem. 1974 Nov 25;249(22):7282-9. PMID:4436310
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