EC Number   |
General Information |
Reference |
|---|
   4.2.1.112 | evolution |
the enzyme belongs to the tungsten containing enzymes, and is a member of the dimethyl sulfoxide reductase (DMSOR) family of enzymes. The W center coordinated by the two MGDs with the [4Fe-4S] cluster in close proximity, is unique for an enzyme of the DMSOR family |
748431 |
| 4.2.1.112 | evolution |
the enzyme belongs to the tungsten containing enzymes, it is a unique W, Fe-S enzyme and a member of the dimethyl sulfoxide reductase (DMSOR) family of enzymes. The W, Fe-S-dependent enzyme might have arosen recently as a means for microbes to take advantage of local anthropogenic sources of acetylene or it represents the relic of some ancestral biochemical process |
748243 |
| 4.2.1.112 | metabolism |
in isoprenoid biosynthesis, the protein (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate reductase performs a 2H+/2e- reduction and deoxygenation of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate, yielding isopentenyl diphosphate and dimethylallyl diphosphate. In addition to its role as a 2H+/2e- reductase in isoprenoid biosynthesis, IspH can catalyse a second class of reactions: the addition of water to acetylene groups to produce aldehyde and ketone products |
730116 |
| 4.2.1.112 | more |
Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme |
748243 |
| 4.2.1.112 | more |
Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme. Active site cavity structure of Pelobacter acetylenicus acetylene hydratase, overview. A C2H2 molecule docked computationally at the AH active site gives an excellent fit in the pocket of the hydrophobic ring with its carbon atoms positioned directly above the oxygen ligand and the carboxylic acid group of active site residue Asp13 |
748431 |
| 4.2.1.112 | more |
Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme. Active site cavity structure of Pelobacter acetylenicus acetylene hydratase, overview. A C2H2 molecule docked computationally at the AH active site gives an excellent fit in the pocket of the hydrophobic ring with its carbon atoms positioned directly above the oxygen ligand and the carboxylic acid group of Asp13 |
748243 |
| 4.2.1.112 | more |
study of the chemoselectivity of tungsten-dependent acetylene hydratase, overview |
713603 |
