EC Number   |
General Information |
Reference |
|---|
  1.1.1.396 | metabolism |
BchC oxidoreductase is involved in bacteriochlorophyll a biosynthesis. The presence of BchC accelerates the 3-vinyl hydration by BchF hydratase of Chlorobaculum tepidum during conversion of chlorophyllide a to 3-acetyl-chlorophyllide a through 3-(1-hydroxyethyl)-chlorophyllide a, indicating that these enzymes work cooperatively to promote efficient bacteriochlorophyll a biosynthesis |
763031 |
| 1.1.1.396 | metabolism |
the enzyme is involved in bacteriochlorophyll a biosynthesis |
763031 |
| 1.1.1.396 | metabolism |
the enzyme is involved in bacteriochlorophyll a biosynthesis. The presence of BchC accelerates the 3-vinyl hydration by BchF hydratase of Chlorobaculum tepidum during conversion of chlorophyllide a to 3-acetyl-chlorophyllide a through 3-(1-hydroxyethyl)-chlorophyllide a, indicating that these enzymes work cooperatively to promote efficient bacteriochlorophyll a biosynthesis |
763031 |
| 1.1.1.396 | physiological function |
BchC of Chlorobaculum tepidum preferentially oxidizes porphyrin-type pigments, 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a, in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. The enzyme catalyzes both the oxidation of 3HE to 3Ac and the reduction of 3Ac to 3HE, the reverse reaction. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. BchC of Rhodobacter capsulatus demonstrates the same 31R-selectivity, suggesting that utilization of 31R-epimers in BchC-catalyzed reductions may be conserved across different phyla of photosynthetic bacteria |
763031 |
| 1.1.1.396 | physiological function |
BchC of Rhodobacter capsulatus preferentially oxidizes porphyrin-type pigments, 31R-3-(1-hydroxyethyl)-chlorophyllide a and 31R-3-(1-hydroxyethyl)-bacteriochlorophyllide a, in the presence of NAD+ to 3-acetylchlorophyllide a and bacteriochlorophyllide a, respectively, leaving the unreacted 31S-epimers. In the reverse reaction, BchC with NADH predominately produces 31R-epimeric alcohols from the 3-acetyl-(bacterio)chlorins. BchC of Chlorobaculum tepidum demonstrates the same 31R-selectivity, suggesting that utilization of 31R-epimers in BchC-catalyzed reductions may be conserved across different phyla of photosynthetic bacteria. The central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction |
763031 |
