1cf3
From Proteopedia
(New page: 200px<br /><applet load="1cf3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cf3, resolution 1.9Å" /> '''GLUCOSE OXIDASE FROM ...) |
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| - | [[Image:1cf3.gif|left|200px]]<br /><applet load="1cf3" size=" | + | [[Image:1cf3.gif|left|200px]]<br /><applet load="1cf3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cf3, resolution 1.9Å" /> | caption="1cf3, resolution 1.9Å" /> | ||
'''GLUCOSE OXIDASE FROM APERGILLUS NIGER'''<br /> | '''GLUCOSE OXIDASE FROM APERGILLUS NIGER'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glucose oxidase is a flavin-dependent enzyme which catalyses the oxidation | + | 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== | ==About this Structure== | ||
| - | 1CF3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] with NAG and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1CF3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CF3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Glucose oxidase]] | [[Category: Glucose oxidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hecht, H | + | [[Category: Hecht, H J.]] |
[[Category: Kalisz, H.]] | [[Category: Kalisz, H.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: oxidoreductase(flavoprotein)]] | [[Category: oxidoreductase(flavoprotein)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:24 2008'' |
Revision as of 10:05, 21 February 2008
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GLUCOSE OXIDASE FROM APERGILLUS NIGER
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
1CF3 is a Single protein structure of sequence from Aspergillus niger with and as ligands. Active as Glucose oxidase, with EC number 1.1.3.4 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
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