1gpe

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[[Image:1gpe.gif|left|200px]]
[[Image:1gpe.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1gpe |SIZE=350|CAPTION= <scene name='initialview01'>1gpe</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1gpe", 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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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/Glucose_oxidase Glucose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.4 1.1.3.4] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1gpe| PDB=1gpe | 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=1gpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gpe OCA], [http://www.ebi.ac.uk/pdbsum/1gpe PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gpe RCSB]</span>
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}}
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'''GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE'''
'''GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE'''
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[[Category: Hendle, J.]]
[[Category: Hendle, J.]]
[[Category: Kalisz, H M.]]
[[Category: Kalisz, H M.]]
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[[Category: oxidoreductase(flavoprotein)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:51:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:48:48 2008''
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Revision as of 14:51, 2 May 2008

Template:STRUCTURE 1gpe

GLUCOSE OXIDASE FROM PENICILLIUM AMAGASAKIENSE


Overview

Glucose oxidase is a flavin-dependent enzyme which catalyses the oxidation of beta-D-glucose by molecular oxygen to delta-gluconolactone and hydrogen peroxide. The structure of the enzyme from Aspergillus niger, previously refined at 2.3 A resolution, has been refined at 1.9 A resolution to an R value of 19.0%, and the structure of the enzyme from Penicillium amagasakiense, which has 65% sequence identity, has been determined by molecular replacement and refined at 1.8 A resolution to an R value of 16.4%. The structures of the partially deglycosylated enzymes have an r.m.s. deviation of 0.7 A for main-chain atoms and show four N-glycosylation sites, with an extended carbohydrate moiety at Asn89. Substrate complexes of the enzyme from A. niger were modelled by force-field methods. The resulting model is consistent with results from site-directed mutagenesis experiments and shows the beta-D-glucose molecule in the active site of glucose oxidase, stabilized by 12 hydrogen bonds and by hydrophobic contacts to three neighbouring aromatic residues and to flavin adenine dinucleotide. Other hexoses, such as alpha-D-glucose, mannose and galactose, which are poor substrates for the enzyme, and 2-deoxy-D-glucose, form either fewer bonds or unfavourable contacts with neighbouring amino acids. Simulation of the complex between the reduced enzyme and the product, delta-gluconolactone, has provided an explanation for the lack of product inhibition by the lactone.

About this Structure

1GPE is a Single protein structure of sequence from Penicillium amagasakiense. The following page contains interesting information on the relation of 1GPE with [Glucose Oxidase]. Full crystallographic information is available from OCA.

Reference

1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes., Wohlfahrt G, Witt S, Hendle J, Schomburg D, Kalisz HM, Hecht HJ, Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):969-77. PMID:10216293 Page seeded by OCA on Fri May 2 17:51:20 2008

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