1nfs: Difference between revisions

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[[Image:1nfs.jpg|left|200px]]
{{Seed}}
[[Image:1nfs.png|left|200px]]


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{{STRUCTURE_1nfs|  PDB=1nfs  |  SCENE=  }}  
{{STRUCTURE_1nfs|  PDB=1nfs  |  SCENE=  }}  


'''STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH NIPP'''
===STRUCTURE AND MECHANISM OF ACTION OF ISOPENTENYLPYROPHOSPHATE-DIMETHYLALLYLPYROPHOSPHATE ISOMERASE: COMPLEX WITH NIPP===




==Overview==
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Isopentenyl diphosphate (IPP):dimethylallyl diphosphate (DMAPP) isomerase is a key enzyme in the biosynthesis of isoprenoids. The reaction involves protonation and deprotonation of the isoprenoid unit and proceeds through a carbocationic transition state. Analysis of the crystal structures (2 A) of complexes of Escherichia coli IPP.DMAPPs isomerase with a transition state analogue (N,N-dimethyl-2-amino-1-ethyl diphosphate) and a covalently attached irreversible inhibitor (3,4-epoxy-3-methyl-1-butyl diphosphate) indicates that Glu-116, Tyr-104, and Cys-67 are involved in the antarafacial addition/elimination of protons during isomerization. This work provides a new perspective about the mechanism of the reaction.
The line below this paragraph, {{ABSTRACT_PUBMED_12540835}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12540835}}


==About this Structure==
==About this Structure==
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[[Category: Wouters, J.]]
[[Category: Wouters, J.]]
[[Category: Complex]]
[[Category: Complex]]
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