EC Number   |
General Information |
Reference |
|---|
   1.2.5.3 | evolution |
CO dehydrogenase is a member of the xanthine oxidase family |
390482 |
| 1.2.5.3 | evolution |
CO dehydrogenase is a prototype of the molybdenum hydroxylase sequence family |
-, 736397 |
| 1.2.5.3 | evolution |
CODH enzymes are classified into two groups, Ni-CODH and Mo-CODH, based on the type of metal in the active center. The Ni-CODH active center is constructed from nickel, iron, and sulfur clusters. Ni-CODH is distributed among anaerobic carboxydotrophs. The Mo-CODH active center contains molybdenum. Aerobic carboxydotrophs use Mo-CODH. The CODH protein isolated from Aeropyrum pernix is a distinct type of archaeal Mo-CODH. Phylogenetic analysis, overview |
-, 725052 |
| 1.2.5.3 | evolution |
despite the unique nature of the binuclear active site of CO dehydrogenase the enzyme is clearly a member of the xanthine oxidase family of molybdenum-containing enzymes |
736514 |
| 1.2.5.3 | evolution |
the enzyme belongs to the molybdenum hydroxylase (xanthine oxidase) family of Mo enzymes |
736513 |
| 1.2.5.3 | evolution |
the enzyme belongs to the noncanonical members of the xanthine oxidase family. The Mo-containing CO dehydrogenase from Oligotropha carboxidovorans and related organisms is distinct from the highly O2-sensitive Ni/Fe-containing CO dehydrogenase from obligate anaerobes such as Clostridum thermoaceticum or Methanosarcina barkerii. Quinones are unusual physiological oxidants for this family of enzymes, the overall fold of the FAD-containing domain of CO dehydrogenase resembles the dehydrogenase rather than the oxidase form of the bovine xanthine oxidoreductase, particularly with regard to the position of the mobile loop referred to above that is involved in the Dto-O conversion, but there are significant differences in the environment of the FAD in CO dehydrogenase and xanthine dehydrogenase. A Lys-Asp pair near the pyrimidine subnucleus of the flavin is preserved, for example, but the positions of the Ile and aromatic residues are reversed, with the Ile on the re side and Tyr (a Phe in the bovine enzyme) on the si side of the isoalloxazine ring |
725197 |
| 1.2.5.3 | evolution |
the enzyme belongs to the XOR family |
-, 735667 |
| 1.2.5.3 | evolution |
the enzyme is a member of the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes that typically catalyse the oxidative hydroxylation of N-heterocyle and aldehyde |
735935 |
| 1.2.5.3 | evolution |
the enzyme is a member of the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes that typically catalyse the oxidative hydroxylation of N-heterocyle and aldehyde substrates |
735935 |
| 1.2.5.3 | evolution |
the Mo- and Cu-containing CO dehydrogenase from Oligotropha carboxydovorans is both mechanistically and structurally distinct from the extremely O2-sensitive Ni- and Fe-containing CO dehydrogenase from organisms such as Moorella thermoacetica or Methanosarcina barkerii. On the basis of overall architecture and sequence homology, the Mo/Cu CO dehydrogenase belongs to the xanthine oxidase family of enzymes but is unique among members of this large and broadly distributed family in several regards: the reaction catalyzed is not formally a hydroxylation reaction involving hydride abstraction from substrate. The enzyme utilizes ubiquinone as the oxidizing substrate rather than O2 or NADas oxidizing substrate, and, most significantly, its unique binuclear active site contains copper as well as molybdenum |
736437 |
