Group:SMART:2010 Pingry SMART Team: Difference between revisions
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== Cofactor specificity == | == Cofactor specificity == | ||
==='''Modifying cofactor specificity, 2,5-diketo-d-gluconic acid reductase'''=== | ==='''Modifying cofactor specificity, 2,5-diketo-d-gluconic acid reductase'''=== | ||
2,5 Diketo-D-gluconic acid reductase (DKGR) is a member of the aldo keto reductase(AKR) family. 2,5-DKGR is found in corynebacterium, the genus classification of soil-dwelling bacteria, and exists in two variants: DKGR A and DKGR B. Both catalyze the reduction of 2,5 diketo-D-gluconic acid to 2Keto-L-gulonic acid, a precursor to L-absorbic acid (Vitamin C), through a series of intermediate chemical steps. Since vitamin C is an essential, main chemical manufactured worldwide, ways to increase efficiency of its production through mutations of cofactor specificity have been studied by Dr. Banta. Significantly, replacing the NADPH cofactor of 2,5-DKGR with NADH has been noted to expedite vitamin C generation because NADH is more stable, commercially less expensive, and more abundant than NADPH. Since DKGR A has a higher thermal stability at 38°C than DKGR B, mutations of amino acids near the cofactor binding site have been made | 2,5 Diketo-D-gluconic acid reductase (DKGR) is a member of the aldo keto reductase(AKR) family. 2,5-DKGR is found in corynebacterium, the genus classification of soil-dwelling bacteria, and exists in two variants: DKGR A and DKGR B. Both catalyze the reduction of 2,5 diketo-D-gluconic acid to 2Keto-L-gulonic acid, a precursor to L-absorbic acid (Vitamin C), through a series of intermediate chemical steps. Since vitamin C is an essential, main chemical manufactured worldwide, ways to increase efficiency of its production through mutations of cofactor specificity have been studied by Dr. Banta. Significantly, replacing the NADPH cofactor of 2,5-DKGR with NADH has been noted to expedite vitamin C generation because NADH is more stable, commercially less expensive, and more abundant than NADPH. Since DKGR A has a higher thermal stability at 38°C than DKGR B, mutations of amino acids near the cofactor binding site have been made for adaption to the preferable NADH cofactor. | ||
<applet load='1a80' size='400' frame='true' align='left' caption='1a80, 2,5-diketo-d-gluconic acid reductase with NADPH (wild-type)' scene='User:Tommie_Hata/2010_Pingry_S.M.A.R.T._Team/1a80-default/2'/> | <applet load='1a80' size='400' frame='true' align='left' caption='1a80, 2,5-diketo-d-gluconic acid reductase with NADPH (wild-type)' scene='User:Tommie_Hata/2010_Pingry_S.M.A.R.T._Team/1a80-default/2'/> | ||
