3bnd

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{{STRUCTURE_3bnd| PDB=3bnd | SCENE= }}
{{STRUCTURE_3bnd| PDB=3bnd | SCENE= }}
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'''Lipoxygenase-1 (Soybean), I553V Mutant'''
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===Lipoxygenase-1 (Soybean), I553V Mutant===
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==Overview==
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This study examines the impact of a series of mutations at position 553 on the kinetic and structural properties of soybean lipoxygenase-1 (SLO-1). The previously uncharacterized mutants reported herein are I553L, I553V, and I553G. High-resolution x-ray studies of these mutants, together with the earlier studied I553A, show almost no structural change in relation to the WT-enzyme. By contrast, a progression in kinetic behavior occurs in which the decrease in the size of the side chain at position 553 leads to an increased importance of donor-acceptor distance sampling in the course of the hydrogen transfer process. These dynamical changes in behavior are interpreted in the context of two general classes of protein motions, preorganization and reorganization, with the latter including the distance sampling modes [Klinman JP (2006) Philos Trans R Soc London Ser B 361:1323-1331; Nagel Z, Klinman JP (2006) Chem Rev 106:3095-3118]. The aggregate data for SLO-1 show how judicious placement of hydrophobic side chains can influence enzyme catalysis via enhanced donor-acceptor hydrogenic wave function overlap.
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{{ABSTRACT_PUBMED_18216254}}
==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Oxylipin biosynthesis]]
[[Category: Oxylipin biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:27:56 2008''

Revision as of 23:28, 27 July 2008

Image:3bnd.png

Template:STRUCTURE 3bnd

Lipoxygenase-1 (Soybean), I553V Mutant

Template:ABSTRACT PUBMED 18216254

About this Structure

3BND is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

Reference

Enzyme structure and dynamics affect hydrogen tunneling: the impact of a remote side chain (I553) in soybean lipoxygenase-1., Meyer MP, Tomchick DR, Klinman JP, Proc Natl Acad Sci U S A. 2008 Jan 29;105(4):1146-51. Epub 2008 Jan 23. PMID:18216254

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