EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.1.1.396 | more |
BchC preferentially oxidizes 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. 31R-selectivity, overview. While most naturally occurring (B)Chls including BChl a have a magnesium ion at the center of the cyclic tetrapyrrole ring, zinc-chelated BChl a has been found in some organisms. BchC exhibits oxidation activity on zinc 3-(1-hydroxyethyl)-pheophorbide (Zn-3HE-Pheide) a, albeit at a low level, where the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The reduction of Zn-3Ac-Pheide a by BchC in the presence of NADH is also observed, predominantly producing the R-epimer of Zn-3HE-Pheide a. The chlorin pigments lacking a central metal, 3HE-Pheide a and 3Ac-Pheide a, are not suitable for substrates of BchC in the presence of NAD+ or NADH, respectively. Thus, the central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction. Determination of the 31-stereochemistry of 3HEChlide a and 3HE-BChlide a, overview |
Chlorobaculum tepidum |
? |
- |
- |
1.1.1.396 | more |
BchC preferentially oxidizes 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. 31R-selectivity, overview. While most naturally occurring (B)Chls including BChl a have a magnesium ion at the center of the cyclic tetrapyrrole ring, zinc-chelated BChl a has been found in some organisms. BchC exhibits oxidation activity on zinc 3-(1-hydroxyethyl)-pheophorbide (Zn-3HE-Pheide) a, albeit at a low level, where the R-epimer is consumed as a substrate to a greater extent than is the S-epimer. The reduction of Zn-3Ac-Pheide a by BchC in the presence of NADH is also observed, predominantly producing the R-epimer of Zn-3HE-Pheide a. The chlorin pigments lacking a central metal, 3HE-Pheide a and 3Ac-Pheide a, are not suitable for substrates of BchC in the presence of NAD+ or NADH, respectively. Thus, the central metal atoms, Mg and Zn, in the substrates are necessary for BchC-catalyzed reaction. Determination of the 31-stereochemistry of 3HEChlide a and 3HE-BChlide a, overview |
Rhodobacter capsulatus |
? |
- |
- |
1.1.1.396 | 2-devinyl-2-(1-hydroxyethyl)chlorophyllide a + NAD+ |
- |
Cereibacter sphaeroides |
2-acetyl-2-devinylchlorophyllide a + NADH + H+ |
- |
? |
1.1.1.396 | 2-devinyl-2-(1-hydroxyethyl)chlorophyllide a + NAD+ |
- |
Cereibacter sphaeroides NCIB 8253 |
2-acetyl-2-devinylchlorophyllide a + NADH + H+ |
- |
? |
1.1.1.396 | 3-(hydroxy)ethyl-13-hydroxy-pheophorbide a + NAD+ |
- |
Chlorobaculum tepidum |
3-acetyl-13-hydroxy-pheophorbide a + NADH + H+ |
- |
? |
1.1.1.396 | 3-(hydroxy)ethyl-13-hydroxy-pheophorbide a + NAD+ |
- |
Chlorobaculum tepidum TLS |
3-acetyl-13-hydroxy-pheophorbide a + NADH + H+ |
- |
? |
1.1.1.396 | 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+ |
- |
Rhodobacter capsulatus |
bacteriochlorophyllide a + NADH + H+ |
- |
? |
1.1.1.396 | 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+ |
- |
Cereibacter sphaeroides |
bacteriochlorophyllide a + NADH + H+ |
- |
? |
1.1.1.396 | 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+ |
- |
Cereibacter sphaeroides NCIB 8253 |
bacteriochlorophyllide a + NADH + H+ |
- |
? |
1.1.1.396 | 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + NAD+ |
- |
Rhodobacter capsulatus B10 |
bacteriochlorophyllide a + NADH + H+ |
- |
? |