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1add
From Proteopedia
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A PRE-TRANSITION STATE MIMIC OF AN ENZYME: X-RAY STRUCTURE OF ADENOSINE DEAMINASE WITH BOUND 1-DEAZA-ADENOSINE AND ZINC-ACTIVATED WATER
Overview
The refined 2.4-A structure of adenosine deaminase, recently discovered to, be a zinc metalloenzyme [Wilson, D. K., Rudolph, F. B., & Quiocho, F. A., (1991) Science 252, 1278-1284], complexed with the ground-state analog, 1-deazaadenosine shows the mode of binding of the analog and, unexpectedly, a zinc-activated water (hydroxide). This structure of a, pre-transition-state mimic, combined with that previously determined for, the complex with 6(R)-hydroxy-1,6-dihydropurine ribonucleoside, a nearly, ideal transition-state analog, sheds new understanding of the precise, stereospecificity and hydrolytic catalysis of an important and, well-characterized member of a large group of zinc metalloenzymes. As both, of these excellent mimics were generated in the active site, they, demonstrate a powerful means of dissecting the course of an enzymatic, reaction by direct crystallographic analysis.
About this Structure
1ADD is a Single protein structure of sequence from Mus musculus with ZN and 1DA as ligands. Active as Adenosine deaminase, with EC number 3.5.4.4 Full crystallographic information is available from OCA.
Reference
A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water., Wilson DK, Quiocho FA, Biochemistry. 1993 Feb 23;32(7):1689-94. PMID:8439534
Page seeded by OCA on Tue Nov 20 10:46:15 2007
