Sandbox Reserved 771: Difference between revisions

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OCA, Elliott Wyatt

Revision as of 04:24, 5 December 2013 view source Elliott Wyatt (talk \| contribs) 42 edits No edit summary ← Older edit		Revision as of 04:25, 5 December 2013 view source Elliott Wyatt (talk \| contribs) 42 edits No edit summary Newer edit →
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	===Glycine Triad===		===Glycine Triad===

	As stated previously, the catalytic active site of GSS is composed of the G-loop, S-loop, and A-loop. The G-loop has been termed the “<scene name='56/564047/Glycine_triad/1~~'><font color='yellow~~'>Glycine Triad~~</font>~~</scene>” due to the contribution of three glycine residues in this loop to the enzymatic activity of GSS – Gly369, Gly370, and Gly371. While all three residues are essential to the activity of the enzyme, kinetic experiments have shown Gly369 and Gly370 to have much more critical roles than Gly371. G369V and G370V variants were found to contain a mere 0.7% and 0.3% of the activity of the wild type GSS enzyme, respectively. G371V mutants still contained approximately 13% of the wild type activity, indicating a level of importance similar to the Asp458 residue of the A-loop. These experimental results suggest that the mechanism of activity interference lies in a decreased ligand binding and failure to close the active site once the ligand has bound.		As stated previously, the catalytic active site of GSS is composed of the G-loop, S-loop, and A-loop. The G-loop has been termed the “<scene name='56/564047/Glycine_triad/1'>Glycine Triad</scene>” due to the contribution of three glycine residues in this loop to the enzymatic activity of GSS – Gly369, Gly370, and Gly371. While all three residues are essential to the activity of the enzyme, kinetic experiments have shown Gly369 and Gly370 to have much more critical roles than Gly371. G369V and G370V variants were found to contain a mere 0.7% and 0.3% of the activity of the wild type GSS enzyme, respectively. G371V mutants still contained approximately 13% of the wild type activity, indicating a level of importance similar to the Asp458 residue of the A-loop. These experimental results suggest that the mechanism of activity interference lies in a decreased ligand binding and failure to close the active site once the ligand has bound.