EC Number |
Cofactor |
Reference |
---|
1.1.9.1 | heme |
- |
678768 |
1.1.9.1 | heme |
binding of pyrroloquinoline quinone induces shifts in the resonances of the methyl groups of the heme porphyrin ring in the oxidized form of the apoenzyme and a shift in the methionine heme ligand resonance of the reduced form of the apoenzyme. A major effect of pyrroloquinoline quinone binding to apo-QH-EDH is a rotation of the methionine ligand of heme c. Pyrroloquinoline quinone becomes tightly bound, the event leading to a compact enzyme conformation which is able to catalyze rapid intramolecular electron transfer |
389956 |
1.1.9.1 | heme |
heme group participates in enzymatic mechanism |
389953 |
1.1.9.1 | heme |
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Low-spin heme protein |
389960 |
1.1.9.1 | heme |
in the crystals, the four hemes in the unit cell have only two different orientations, related by an 180° rotation about the b axis. The heme rings are oriented parallel to the b axis |
701480 |
1.1.9.1 | heme c |
both isoforms ADH IIB and ADH IIG |
687362 |
1.1.9.1 | pyrroloquinoline quinone |
- |
389953 |
1.1.9.1 | pyrroloquinoline quinone |
binding of pyrroloquinoline quinone induces shifts in the resonances of the methyl groups of the heme porphyrin ring in the oxidized form of the apoenzyme and a shift in the methionine heme ligand resonance of the reduced form of the apoenzyme. A major effect of pyrroloquinoline quinone binding to apo-QH-EDH is a rotation of the methionine ligand of heme c. Pyrroloquinoline quinone becomes tightly bound, the event leading to a compact enzyme conformation which is able to catalyze rapid intramolecular electron transfer |
389956 |
1.1.9.1 | pyrroloquinoline quinone |
both isoforms ADH IIB and ADH IIG |
687362 |
1.1.9.1 | pyrroloquinoline quinone |
holoenzyme contains equimolar amounts of pyrroloquinoline quinone, Ca2+ and covalently bound heme. Reconstitution of apoenzyme with pyrroloquinoline quinone analogues results in a decreased activity and enantioselectivity for the oxidation of chiral alcohols. Possession of the o-quinone or o-quinol moiety is not essential for binding but it is for activity |
389960 |