Adenylosuccinate Synthetase
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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.<ref>PMID:8244965</ref> | 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.<ref>PMID:8244965</ref> | ||
| - | Helices are highlighted in green<scene name='Sandbox_187/Green_helices/1'>here</scene> and beta sheets are shown in orange<scene name='Sandbox_187/Beta_sheets/1'>here</scene>. | + | Helices are highlighted in green <scene name='Sandbox_187/Green_helices/1'>here</scene> and beta sheets are shown in orange <scene name='Sandbox_187/Beta_sheets/1'>here</scene>. |
==Reaction Mechanism== | ==Reaction Mechanism== | ||
Revision as of 03:47, 28 March 2010
Adenylosuccinate Synthetase
Contents |
Introduction
Adenylosuccinate Synthetase (AdSS) is an enzyme that is mainly involved in purine bio-synthesis. It does this by catalyzing the GTP dependent changeover of IMP and aspartic acid to AMP. [1]
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.[2]
Helices are highlighted in green and beta sheets are shown in orange .
Reaction Mechanism
References
- ↑ Mukhopadhyay RP, Chandra AL. Keratinase of a streptomycete. Indian J Exp Biol. 1990 Jun;28(6):575-7. PMID:1698173
- ↑ 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
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