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On the role of Glu‐68 in alcohol dehydrogenase

Ryde, Ulf LU (1995) In Protein Science 4(6). p.1124-1132
Abstract

Theoretical computations (molecular dynamics and combined quantum chemical and molecular mechanical geometry optimizations) have been performed on horse liver alcohol dehydrogenase. The results provide evidence that Glu‐68, a highly conserved residue located 0.47 nm from the catalytic zinc ion, may intermittently coordinate to the zinc ion. Structures with Glu‐68 coordinated to the zinc ion are almost as stable as structures with Glu‐68 at the crystal position and the barrier between the two configurations of Glu‐68 is so low that it can readily be bypassed at room temperature. There is a cavity behind the zinc ion that seems to be tailored to allow such coordination of Glu‐68 to the zinc ion. It is suggested that Glu‐68 may facilitate... (More)

Theoretical computations (molecular dynamics and combined quantum chemical and molecular mechanical geometry optimizations) have been performed on horse liver alcohol dehydrogenase. The results provide evidence that Glu‐68, a highly conserved residue located 0.47 nm from the catalytic zinc ion, may intermittently coordinate to the zinc ion. Structures with Glu‐68 coordinated to the zinc ion are almost as stable as structures with Glu‐68 at the crystal position and the barrier between the two configurations of Glu‐68 is so low that it can readily be bypassed at room temperature. There is a cavity behind the zinc ion that seems to be tailored to allow such coordination of Glu‐68 to the zinc ion. It is suggested that Glu‐68 may facilitate the exchange of ligands in the substrate site by coordinating to the zinc ion when the old ligand dissociates. Copyright © 2000 The Protein Society

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author
organization
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type
Contribution to journal
publication status
published
subject
keywords
combined ab initio, five‐coordination, geometry imposed by enzyme, ligand exchange, molecular dynamics, molecular mechanical geometry optimization, reaction mechanism
in
Protein Science
volume
4
issue
6
pages
9 pages
publisher
The Protein Society
external identifiers
  • scopus:0029033663
ISSN
0961-8368
DOI
10.1002/pro.5560040611
language
English
LU publication?
no
id
0f2a203a-bbd2-4991-8425-c598ea8df31c
date added to LUP
2017-02-04 11:32:25
date last changed
2017-05-01 20:47:12
@article{0f2a203a-bbd2-4991-8425-c598ea8df31c,
  abstract     = {<p>Theoretical computations (molecular dynamics and combined quantum chemical and molecular mechanical geometry optimizations) have been performed on horse liver alcohol dehydrogenase. The results provide evidence that Glu‐68, a highly conserved residue located 0.47 nm from the catalytic zinc ion, may intermittently coordinate to the zinc ion. Structures with Glu‐68 coordinated to the zinc ion are almost as stable as structures with Glu‐68 at the crystal position and the barrier between the two configurations of Glu‐68 is so low that it can readily be bypassed at room temperature. There is a cavity behind the zinc ion that seems to be tailored to allow such coordination of Glu‐68 to the zinc ion. It is suggested that Glu‐68 may facilitate the exchange of ligands in the substrate site by coordinating to the zinc ion when the old ligand dissociates. Copyright © 2000 The Protein Society</p>},
  author       = {Ryde, Ulf},
  issn         = {0961-8368},
  keyword      = {combined ab initio,five‐coordination,geometry imposed by enzyme,ligand exchange,molecular dynamics,molecular mechanical geometry optimization,reaction mechanism},
  language     = {eng},
  number       = {6},
  pages        = {1124--1132},
  publisher    = {The Protein Society},
  series       = {Protein Science},
  title        = {On the role of Glu‐68 in alcohol dehydrogenase},
  url          = {http://dx.doi.org/10.1002/pro.5560040611},
  volume       = {4},
  year         = {1995},
}