EC number:1.1.5.9
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.5 With a quinone or similar compound as acceptor |
| ID: | 1.1.5.9 | ||
|---|---|---|---|
| Description: | Glucose 1-dehydrogenase (FAD, quinone). | ||
| Alternative Name: |
Glucose dehydrogenase (Aspergillus). FAD-dependent glucose dehydrogenase. | ||
| Prosite: | PDOC00543; | ||
| PDB: |
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3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.5.9 |
| BRENDA Enzyme Link: | BRENDA 1.1.5.9 |
| KEGG Enzyme Link: | KEGG1.1.5.9 |
| BioCyc Enzyme Link: | BioCyc 1.1.5.9 |
| ExPASy Enzyme Link: | ExPASy1.1.5.9 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.5.9 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.5.9 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.5.9 |
| IntEnz Enzyme Link: | IntEnz 1.1.5.9 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.5.9 |
| RHEA:47372 | a quinone + D-glucose = a quinol + D-glucono-1,5-lactone |
| RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5](=[O;H0;+0:6])-[C;H0;+0:7](-[*:8])=[C;H0;+0:9](-[*:10])-[C;H0;+0:11]-1=[O;H0;+0:12].[*:13]-[CH;+0:14](-[*:15])-[OH;+0:16]>>[*:13]-[C;H0;+0:14](-[*:15])=[O;H0;+0:16].[*:1]-[c;H0;+0:2]1:[c;H0;+0:11](-[OH;+0:12]):[c;H0;+0:9](-[*:10]):[c;H0;+0:7](-[*:8]):[c;H0;+0:5](-[OH;+0:6]):[c;H0;+0:3]:1-[*:4] |
| Reaction |  |
| Core-to-Core | |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Biphasic expression and function of glucose dehydrogenase in Drosophila melanogaster. | Cavener DR, MacIntyre RJ | 1983 Oct | 6413974 |
| Studies on glucose dehydrogenase of Aspergillus oryzae. II. Purification and physical and chemical properties. | Bak TG | 1967 Jul 11 | 6034674 |
| Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris. | Sygmund C, Staudigl P, Klausberger M, Pinotsis N, Djinović-Carugo K, Gorton L, Haltrich D, Ludwig R | 2011 Dec 12 | 22151971 |
| Reduction of quinones and phenoxy radicals by extracellular glucose dehydrogenase from Glomerella cingulata suggests a role in plant pathogenicity. | Sygmund C, Klausberger M, Felice AK, Ludwig R | 2011 Nov | 21903757 |
| Alteration in FAD-glucose dehydrogenase activity and hemocyte behavior contribute to initial disruption of Manduca sexta immune response to Cotesia congregata parasitoids. | Lovallo N, Cox-Foster DL | 1999 Dec | 12770264 |
| Cloning and expression of the gene encoding catalytic subunit of thermostable glucose dehydrogenase from Burkholderia cepacia in Escherichia coli. | Inose K, Fujikawa M, Yamazaki T, Kojima K, Sode K | 2003 Feb 21 | 12573242 |