1u2y: Difference between revisions

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==Overview==

A new approach for the discovery and subsequent structural elucidation of, oligosaccharide-based inhibitors of alpha-amylases based upon, autoglucosylation of known alpha-glucosidase inhibitors is presented. This, concept, highly analogous to what is hypothesized to occur with acarbose, is demonstrated with the known alpha-glucosidase inhibitor, d-gluconohydroximino-1,5-lactam. This was transformed from an inhibitor of, human pancreatic alpha-amylase with a K(i) value of 18 mm to a, trisaccharide analogue with a K(i) value of 25 mum. The three-dimensional, structure of this complex was determined by x-ray crystallography and, represents the first such structure determined with this class of, inhibitors in any alpha-glycosidase. This approach to the discovery and, structural analysis of amylase inhibitors should be generally applicable, to other endoglucosidases and readily adaptable to a high throughput, format.

A new approach for the discovery and subsequent structural elucidation of oligosaccharide-based inhibitors of alpha-amylases based upon autoglucosylation of known alpha-glucosidase inhibitors is presented. This concept, highly analogous to what is hypothesized to occur with acarbose, is demonstrated with the known alpha-glucosidase inhibitor, d-gluconohydroximino-1,5-lactam. This was transformed from an inhibitor of human pancreatic alpha-amylase with a K(i) value of 18 mm to a trisaccharide analogue with a K(i) value of 25 mum. The three-dimensional structure of this complex was determined by x-ray crystallography and represents the first such structure determined with this class of inhibitors in any alpha-glycosidase. This approach to the discovery and structural analysis of amylase inhibitors should be generally applicable to other endoglucosidases and readily adaptable to a high throughput format.

==About this Structure==

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[[Category: Single protein]]

[[Category: Begum, A.]]

[[Category: Brayer, G.D.]]

[[Category: Brayer, G D.]]

[[Category: Damager, I.]]

[[Category: Li, C.]]

[[Category: Numao, S.]]

[[Category: Overall, C.M.]]

[[Category: Overall, C M.]]

[[Category: Withers, S.G.]]

[[Category: Withers, S G.]]

[[Category: Wrodnigg, T.M.]]

[[Category: Wrodnigg, T M.]]

[[Category: CA]]

[[Category: CL]]

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[[Category: inhibitor]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:20 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-A new approach for the discovery and subsequent structural elucidation of, oligosaccharide-based inhibitors of alpha-amylases based upon, autoglucosylation of known alpha-glucosidase inhibitors is presented. This, concept, highly analogous to what is hypothesized to occur with acarbose, is demonstrated with the known alpha-glucosidase inhibitor, d-gluconohydroximino-1,5-lactam. This was transformed from an inhibitor of, human pancreatic alpha-amylase with a K(i) value of 18 mm to a, trisaccharide analogue with a K(i) value of 25 mum. The three-dimensional, structure of this complex was determined by x-ray crystallography and, represents the first such structure determined with this class of, inhibitors in any alpha-glycosidase. This approach to the discovery and, structural analysis of amylase inhibitors should be generally applicable, to other endoglucosidases and readily adaptable to a high throughput, format.
+A new approach for the discovery and subsequent structural elucidation of oligosaccharide-based inhibitors of alpha-amylases based upon autoglucosylation of known alpha-glucosidase inhibitors is presented. This concept, highly analogous to what is hypothesized to occur with acarbose, is demonstrated with the known alpha-glucosidase inhibitor, d-gluconohydroximino-1,5-lactam. This was transformed from an inhibitor of human pancreatic alpha-amylase with a K(i) value of 18 mm to a trisaccharide analogue with a K(i) value of 25 mum. The three-dimensional structure of this complex was determined by x-ray crystallography and represents the first such structure determined with this class of inhibitors in any alpha-glycosidase. This approach to the discovery and structural analysis of amylase inhibitors should be generally applicable to other endoglucosidases and readily adaptable to a high throughput format.
 ==About this Structure==
@@ Line 15: / Line 15: @@
 [[Category: Single protein]]
 [[Category: Begum, A.]]
-[[Category: Brayer, G.D.]]
+[[Category: Brayer, G D.]]
 [[Category: Damager, I.]]
 [[Category: Li, C.]]
 [[Category: Numao, S.]]
-[[Category: Overall, C.M.]]
+[[Category: Overall, C M.]]
-[[Category: Withers, S.G.]]
+[[Category: Withers, S G.]]
-[[Category: Wrodnigg, T.M.]]
+[[Category: Wrodnigg, T M.]]
 [[Category: CA]]
 [[Category: CL]]
@@ Line 33: / Line 33: @@
 [[Category: inhibitor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:59:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:20 2008''