Glucose-methanol-choline oxidoreductase family explained
| Symbol: | GMC_oxred_N |
| GMC oxidoreductase |
| Pfam: | PF00732 |
| Pfam Clan: | CL0063 |
| Interpro: | IPR000172 |
| Prosite: | PDOC00543 |
| Scop: | 1gal |
| Opm Family: | 132 |
| Opm Protein: | 1b4v |
| Symbol: | GMC_oxred_C |
| GMC oxidoreductase |
| Pfam: | PF05199 |
| Interpro: | IPR007867 |
| Prosite: | PDOC00543 |
| Scop: | 1gal |
In molecular biology, the glucose-methanol-choline oxidoreductase family (GMC oxidoreductase) is a family of enzymes with oxidoreductase activity.
The glucose-methanol-choline (GMC) oxidoreductases are FAD flavoproteins oxidoreductases.[1] [2] These enzymes include a variety of proteins; choline dehydrogenase (CHD), methanol oxidase (MOX) and cellobiose dehydrogenase [3] which share a number of regions of sequence similarities. They contain two conserved protein domains. The N-terminal domain corresponds to the FAD ADP-binding domain, the C-terminal domain is a steroid-binding domain.[4] [5]
Notes and References
- Cavener DR . GMC oxidoreductases. A newly defined family of homologous proteins with diverse catalytic activities . J. Mol. Biol. . 223 . 3 . 811–4 . February 1992 . 1542121 . 10.1016/0022-2836(92)90992-S.
- Li J, Vrielink A, Brick P, Blow DM . Alice Vrielink. Crystal structure of cholesterol oxidase complexed with a steroid substrate: implications for flavin adenine dinucleotide dependent alcohol oxidases . Biochemistry . 32 . 43 . 11507–15 . November 1993 . 8218217 . 10.1021/bi00094a006.
- Henriksson G, Johansson G, Pettersson G . A critical review of cellobiose dehydrogenases . J. Biotechnol. . 78 . 2 . 93–113 . March 2000 . 10725534 . 10.1016/S0168-1656(00)00206-6.
- Bannwarth M, Bastian S, Heckmann-Pohl D, Giffhorn F, Schulz GE . Crystal structure of pyranose 2-oxidase from the white-rot fungus Peniophora sp. . Biochemistry . 2004 . 43 . 37 . 11683–90 . 15362852 . 10.1021/bi048609q .
- Vrielink A, Lloyd LF, Blow DM . Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 A resolution. . Alice Vrielink. J Mol Biol . 1991 . 219 . 3 . 533–54 . 2051487 . 10.1016/0022-2836(91)90192-9.
