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1xd0

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[[Image:1xd0.gif|left|200px]]
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{{STRUCTURE_1xd0| PDB=1xd0 | SCENE= }}
{{STRUCTURE_1xd0| PDB=1xd0 | SCENE= }}
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'''Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts'''
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===Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts===
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==Overview==
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A mechanistic study of the poorly understood pathway by which the inhibitor acarbose is enzymatically rearranged by human pancreatic alpha-amylase has been conducted by structurally examining the binding modes of the related inhibitors isoacarbose and acarviosine-glucose, and by novel kinetic measurements of all three inhibitors under conditions that demonstrate this rearrangement process. Unlike acarbose, isoacarbose has a unique terminal alpha-(1-6) linkage to glucose and is found to be resistant to enzymatic rearrangement. This terminal glucose unit is found to bind in the +3 subsite and for the first time reveals the interactions that occur in this part of the active site cleft with certainty. These results also suggest that the +3 binding subsite may be sufficiently flexible to bind the alpha-(1-6) branch points in polysaccharide substrates, and therefore may play a role in allowing efficient cleavage in the direct vicinity of such junctures. Also found to be resistant to enzymatic rearrangement was acarviosine-glucose, which has one fewer glucose unit than acarbose. Collectively, structural studies of all three inhibitors and the specific cleavage pattern of HPA make it possible to outline the simplest sequence of enzymatic reactions likely involved upon acarbose binding. Prominent features incorporated into the starting structure of acarbose to facilitate the synthesis of the final tightly bound pseudo-pentasaccharide product are the restricted availability of hydrolyzable bonds and the placement of the transition state-like acarviosine group. Additional "in situ" experiments designed to elongate and thereby optimize isoacarbose and acarviosine-glucose inhibition using the activated substrate alphaG3F demonstrate the feasibility of this approach and that the principles outlined for acarbose rearrangement can be used to predict the final products that were obtained.
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(as it appears on PubMed at http://www.pubmed.gov), where 15736945 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15736945}}
==About this Structure==
==About this Structure==
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[[Category: Isoacarbose]]
[[Category: Isoacarbose]]
[[Category: Structure]]
[[Category: Structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:52:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:19:42 2008''

Revision as of 15:19, 27 July 2008

Image:1xd0.png

Template:STRUCTURE 1xd0

Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts

Template:ABSTRACT PUBMED 15736945

About this Structure

1XD0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts., Li C, Begum A, Numao S, Park KH, Withers SG, Brayer GD, Biochemistry. 2005 Mar 8;44(9):3347-57. PMID:15736945

Page seeded by OCA on Sun Jul 27 18:19:42 2008

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