Accepted Name |
chlorophyllide a reductase
|
Reaction catalysed |
- 3-deacetyl-3-vinylbacteriochlorophyllide a + ADP + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate <=> ATP + chlorophyllide a + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin]
- ADP + bacteriochlorophyllide a + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate <=> 3-acetyl-3-devinylchlorophyllide a + ATP + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin]
- 3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + ADP + 2 oxidized [2Fe-2S]-[ferredoxin] + phosphate <=> 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + ATP + H(+) + H2O + 2 reduced [2Fe-2S]-[ferredoxin]
|
Comment(s) |
- The enzyme, together with EC 1.1.1.396 and EC 4.2.1.165, is involved
in the conversion of chlorophyllide a to bacteriochlorophyllide a.
- These enzymes can act in multiple orders, resulting in the formation
of different intermediates, but the final product of the cumulative
action of the three enzymes is always bacteriochlorophyllide a.
- This enzyme catalyzes a trans-reduction of the B-ring; the product
has the (7R,8R)-configuration.
- In addition, the enzyme has a latent activity of EC 1.3.7.13.
- Formerly EC 1.3.99.35.
|
Cross-references |
BRENDA | 1.3.7.15 |
EC2PDB | 1.3.7.15 |
ExplorEnz | 1.3.7.15 |
PRIAM enzyme-specific profiles | 1.3.7.15 |
KEGG Ligand Database for Enzyme Nomenclature | 1.3.7.15 |
IUBMB Enzyme Nomenclature | 1.3.7.15 |
IntEnz | 1.3.7.15 |
MEDLINE | Find literature relating to 1.3.7.15 |
MetaCyc | 1.3.7.15 |
Rhea expert-curated reactions | 1.3.7.15 |
UniProtKB/Swiss-Prot |
Q02431, BCHX_CERS4 | P26177, BCHX_RHOCB | Q02432, BCHY_CERS4 |
P26178, BCHY_RHOCB | Q3J1A0, BCHZ_CERS4 | P0C0X6, BCHZ_CERSP |
Q9KWI8, BCHZ_ERYLO | P26179, BCHZ_RHOCB | P26277, BCHZ_ROSDO |
Q9JPB9, BCHZ_RUBGI |
|
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UniProtKB/Swiss-Prot entries corresponding to 1.3.7.-
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