1ocq: Difference between revisions

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==Overview==

Glycosidases are some of the most ubiquitous enzyme in nature. Their, biological significance, coupled to their enormous catalytic prowess, derived from tight binding of the transition state, is reflected in their, importance as therapeutic targets. Many glycosidase inhibitors are known., Imino sugars are often potent inhibitors, yet many facets of their mode of, action, such as their degree, if any, of transition-state "mimicry" and, their protonation state when bound to the target glycosidase remain, unclear. Atomic resolution analysis of the endoglucanase, Cel5A, in, complex with a cellobio-derived isofagomine in conjunction with the pH, dependence of Ki and kcat/KM reveals that this compound binds as a, protonated sugar. Surprisingly, both the enzymatic nucleophile and the, acid/base are unprotonated in the complex.

Glycosidases are some of the most ubiquitous enzyme in nature. Their biological significance, coupled to their enormous catalytic prowess derived from tight binding of the transition state, is reflected in their importance as therapeutic targets. Many glycosidase inhibitors are known. Imino sugars are often potent inhibitors, yet many facets of their mode of action, such as their degree, if any, of transition-state "mimicry" and their protonation state when bound to the target glycosidase remain unclear. Atomic resolution analysis of the endoglucanase, Cel5A, in complex with a cellobio-derived isofagomine in conjunction with the pH dependence of Ki and kcat/KM reveals that this compound binds as a protonated sugar. Surprisingly, both the enzymatic nucleophile and the acid/base are unprotonated in the complex.

==About this Structure==

Line 14:

[[Category: Cellulase]]

[[Category: Single protein]]

[[Category: Davies, G.J.]]

[[Category: Davies, G J.]]

[[Category: Macdonald, J.]]

[[Category: Stick, R.V.]]

[[Category: Stick, R V.]]

[[Category: Varrot, A.]]

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

[[Category: Withers, S G.]]

[[Category: BGC]]

[[Category: GOL]]

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[[Category: hydrolase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:14 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Glycosidases are some of the most ubiquitous enzyme in nature. Their, biological significance, coupled to their enormous catalytic prowess, derived from tight binding of the transition state, is reflected in their, importance as therapeutic targets. Many glycosidase inhibitors are known., Imino sugars are often potent inhibitors, yet many facets of their mode of, action, such as their degree, if any, of transition-state "mimicry" and, their protonation state when bound to the target glycosidase remain, unclear. Atomic resolution analysis of the endoglucanase, Cel5A, in, complex with a cellobio-derived isofagomine in conjunction with the pH, dependence of Ki and kcat/KM reveals that this compound binds as a, protonated sugar. Surprisingly, both the enzymatic nucleophile and the, acid/base are unprotonated in the complex.
+Glycosidases are some of the most ubiquitous enzyme in nature. Their biological significance, coupled to their enormous catalytic prowess derived from tight binding of the transition state, is reflected in their importance as therapeutic targets. Many glycosidase inhibitors are known. Imino sugars are often potent inhibitors, yet many facets of their mode of action, such as their degree, if any, of transition-state "mimicry" and their protonation state when bound to the target glycosidase remain unclear. Atomic resolution analysis of the endoglucanase, Cel5A, in complex with a cellobio-derived isofagomine in conjunction with the pH dependence of Ki and kcat/KM reveals that this compound binds as a protonated sugar. Surprisingly, both the enzymatic nucleophile and the acid/base are unprotonated in the complex.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Cellulase]]
 [[Category: Single protein]]
-[[Category: Davies, G.J.]]
+[[Category: Davies, G J.]]
 [[Category: Macdonald, J.]]
-[[Category: Stick, R.V.]]
+[[Category: Stick, R V.]]
 [[Category: Varrot, A.]]
-[[Category: Withers, S.G.]]
+[[Category: Withers, S G.]]
 [[Category: BGC]]
 [[Category: GOL]]
@@ Line 28: / Line 28: @@
 [[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:56:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:14 2008''