1did

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[[Image:1did.jpg|left|200px]]
[[Image:1did.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1did |SIZE=350|CAPTION= <scene name='initialview01'>1did</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1did", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=DIG:2,5-DIDEOXY-2,5-IMINO-D-GLUCITOL'>DIG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Xylose_isomerase Xylose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.5 5.3.1.5] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1did| PDB=1did | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1did FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1did OCA], [http://www.ebi.ac.uk/pdbsum/1did PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1did RCSB]</span>
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}}
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'''OBSERVATIONS OF REACTION INTERMEDIATES AND THE MECHANISM OF ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE'''
'''OBSERVATIONS OF REACTION INTERMEDIATES AND THE MECHANISM OF ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE'''
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[[Category: Collyer, C A.]]
[[Category: Collyer, C A.]]
[[Category: Goldberg, J D.]]
[[Category: Goldberg, J D.]]
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[[Category: isomerase(intramolecular oxidoreductse)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:52:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:42:05 2008''
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Revision as of 10:52, 2 May 2008

Image:1did.jpg

Template:STRUCTURE 1did

OBSERVATIONS OF REACTION INTERMEDIATES AND THE MECHANISM OF ALDOSE-KETOSE INTERCONVERSION BY D-XYLOSE ISOMERASE


Overview

Crystallographic studies of D-xylose isomerase (D-xylose ketol-isomerase, EC 5.3.1.5) incubated to equilibrium with substrate/product mixtures of xylose and xylulose show electron density for a bound intermediate. The accumulation of this bound intermediate shows that the mechanism is a non-Michaelis type. Carrell et al. [Carrell, H. L., Glusker, J. P., Burger, V., Manfre, F., Tritsch, D. & Biellmann, J.-F. (1989) Proc. Natl. Acad. Sci. USA 86, 4440-4444] and the present authors studied crystals of the enzyme-substrate complex under different conditions and made different interpretations of the substrate density, leading to different conclusions about the enzyme mechanism. All authors agree that the bound intermediate of the sugar is in an open-chain form. It is suggested that the higher-temperature study of Carrell et al. may have produced an equilibrium of multiple states, whose density fits poorly to the open-chain substrate, and led to incorrect interpretation. The two groups also bound different closed-ring sugar analogues to the enzyme, but these analogues bind differently. A possible explanation consistent with all the data is that the enzyme operates by a hydride shift mechanism.

About this Structure

1DID is a Single protein structure of sequence from Arthrobacter sp.. Full crystallographic information is available from OCA.

Reference

Observations of reaction intermediates and the mechanism of aldose-ketose interconversion by D-xylose isomerase., Collyer CA, Blow DM, Proc Natl Acad Sci U S A. 1990 Feb;87(4):1362-6. PMID:2304904 Page seeded by OCA on Fri May 2 13:52:38 2008

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