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Literature summary for 1.3.7.15 extracted from

  • Azai, C.; Kobayashi, M.; Mizoguchi, T.; Tamiaki, H.; Terauchi, K.; Tsukatani, Y.
    Rapid C8-vinyl reduction of divinyl-chlorophyllide a by BciA from Rhodobacter capsulatus (2018), J. Photochem. Photobiol. A, 353, 661-666 .
No PubMed abstract available
Search for more literature for 1.3.7.15

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information oligomeric BciA provides a kcat/Km value of 0.029/s * microM, which is 15fold higher than the value of a-COR towards Chlide a (0.0019/s * microM when the ratio of BchX:BchYZ is 4:1) Rhodobacter capsulatus
0.0059
-
 8-vinyl chlorophyllide a pH 8.0, 22°C, recombinant BchYZ heterodimer Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+ Rhodobacter capsulatus
-
 bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
 ?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+ Rhodobacter capsulatus NBRC 16581
-
 bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
 ?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+ Rhodobacter capsulatus ATCC BAA-309
-
 bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
 ?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+ Rhodobacter capsulatus SB1003
-
 bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
 ?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Rhodobacter capsulatus
-
 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Rhodobacter capsulatus NBRC 16581
-
 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Rhodobacter capsulatus ATCC BAA-309
-
 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Rhodobacter capsulatus SB1003
-
 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus P26177 AND P26178 AND P26179 genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
-
Rhodobacter capsulatus ATCC BAA-309 P26177 AND P26178 AND P26179 genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
-
Rhodobacter capsulatus NBRC 16581 P26177 AND P26178 AND P26179 genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
-
Rhodobacter capsulatus SB1003 P26177 AND P26178 AND P26179 genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
-
 Rhodobacter capsulatus bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
 ?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
-
 Rhodobacter capsulatus NBRC 16581 bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
 ?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
-
 Rhodobacter capsulatus ATCC BAA-309 bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
 ?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
-
 Rhodobacter capsulatus SB1003 bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
 ?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Rhodobacter capsulatus chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Rhodobacter capsulatus NBRC 16581 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Rhodobacter capsulatus ATCC BAA-309 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Rhodobacter capsulatus SB1003 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?

Subunits

Subunits Comment Organism
More one BchYZ heterodimer is assumed as a minimal active protomer Rhodobacter capsulatus

Synonyms

Synonyms Comment Organism
a-COR
-
 Rhodobacter capsulatus
BchX
-
 Rhodobacter capsulatus
BchY
-
 Rhodobacter capsulatus
BchZ
-
 Rhodobacter capsulatus
COR
-
 Rhodobacter capsulatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Rhodobacter capsulatus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.011
-
 8-vinyl chlorophyllide a pH 8.0, 22°C, recombinant BchYZ heterodimer Rhodobacter capsulatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Rhodobacter capsulatus

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Rhodobacter capsulatus
Fe-S center
-
 Rhodobacter capsulatus
Ferredoxin
-
 Rhodobacter capsulatus

General Information

General Information Comment Organism
evolution BciA (EC 1.3.1.75, NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR, BciA from Rhodobacter capsulatus has a lower affinity for DV-Chlide a but a much higher specific activity Rhodobacter capsulatus
physiological function chlorophyllide (Chlide) oxidoreductase, COR, is a unique BChl biosynthesis enzyme which shows distinct substrate recognition and hydrogen addition activities, depending on the host strain. COR in BChl a-producing phototrophic bacteria (a-COR) catalyzes the C7=C8 double bond reduction of Chlide a, whereas COR in BChl b- and BChl g-producing bacteria (b/g-COR) forms the C8-ethylidene group using DV-Chlide a as the substrate. Chlorophyllide oxidoreductase (COR) reduces the C7=C8 double bond of chlorophyllide a (Chlide a) bearing the C8-ethyl group, but also potentially catalyzes the reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms Rhodobacter capsulatus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.864
-
 8-vinyl chlorophyllide a pH 8.0, 22°C, recombinant BchYZ heterodimer Rhodobacter capsulatus