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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.75 expressed in Escherichia coli Rosetta2 cells Rhodobacter capsulatus
1.3.1.75 gene bciA or RCAP_rcc03260, DNA and amino acid sequence determination and analysis, recombinant expression of N-terminally Strep II-tagged enzyme in Escherichia coli strain Rosetta 2 Rhodobacter capsulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.75 additional information
-
 additional information Lineweaver-Burk plots, For the assay using BciA prepared under the high-salt condition (1.0 M NaCl), the assay buffer is supplemented with 1.0 M NaCl Rhodobacter capsulatus
1.3.1.75 0.023
-
 3,8-divinyl chlorophyllide a pH 8.0, 22°C, recombinant Strep II-tagged oligomeric enzyme, low salt condition Rhodobacter capsulatus
1.3.1.75 0.023
-
 3,8-divinyl protochlorophyllide a oligomeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C Rhodobacter capsulatus
1.3.1.75 0.032
-
 3,8-divinyl chlorophyllide a pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, low salt condition Rhodobacter capsulatus
1.3.1.75 0.032
-
 3,8-divinyl protochlorophyllide a dimeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C Rhodobacter capsulatus
1.3.1.75 0.035
-
 3,8-divinyl chlorophyllide a pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, high salt condition Rhodobacter capsulatus
1.3.1.75 0.035
-
 3,8-divinyl protochlorophyllide a dimeric enzyme (high salt condition, 1 M NaCl), at pH 8.0 and 25°C Rhodobacter capsulatus
1.3.7.15 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
1.3.7.15 0.0059
-
 8-vinyl chlorophyllide a pH 8.0, 22°C, recombinant BchYZ heterodimer Rhodobacter capsulatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.75 additional information
-
 since the oligomeric BciA eluted from the Sephacryl S-200HR column is estimated to have a mass above 200 kDa, it is a hexamer or larger complex Rhodobacter capsulatus
1.3.1.75 200000
-
 gel filtration Rhodobacter capsulatus
1.3.1.75 200000
-
 above, recombinant N-terminally Strep II-tagged enzyme BciA, gel filtration Rhodobacter capsulatus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ Rhodobacter capsulatus
-
 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ Rhodobacter capsulatus NBRC 16581
-
 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ Rhodobacter capsulatus ATCC BAA-309
-
 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ Rhodobacter capsulatus SB1003
-
 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+ Rhodobacter capsulatus
-
 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+ Rhodobacter capsulatus NBRC 16581
-
 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+ Rhodobacter capsulatus ATCC BAA-309
-
 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+ Rhodobacter capsulatus SB1003
-
 protochlorophyllide a + NADP+
-
 ?
1.3.7.15 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
-
 ?
1.3.7.15 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
-
 ?
1.3.7.15 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
-
 ?
1.3.7.15 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
-
 ?
1.3.7.15 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Rhodobacter capsulatus
-
 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.7.15 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Rhodobacter capsulatus NBRC 16581
-
 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.7.15 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
-
 ?
1.3.7.15 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Rhodobacter capsulatus SB1003
-
 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.75 Rhodobacter capsulatus
-
-
-
1.3.1.75 Rhodobacter capsulatus D5ARW2
-
-
1.3.1.75 Rhodobacter capsulatus ATCC BAA-309 D5ARW2
-
-
1.3.1.75 Rhodobacter capsulatus NBRC 16581 D5ARW2
-
-
1.3.1.75 Rhodobacter capsulatus SB1003
-
-
-
1.3.1.75 Rhodobacter capsulatus SB1003 D5ARW2
-
-
1.3.7.15 Rhodobacter capsulatus P26177 AND P26178 AND P26179 genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
-
1.3.7.15 Rhodobacter capsulatus ATCC BAA-309 P26177 AND P26178 AND P26179 genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
-
1.3.7.15 Rhodobacter capsulatus NBRC 16581 P26177 AND P26178 AND P26179 genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
-
1.3.7.15 Rhodobacter capsulatus SB1003 P26177 AND P26178 AND P26179 genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.75 recombinant N-terminally Strep II-tagged enzyme from Escherichia coli strain Rosetta 2 by affinity chromatography and gel filtration Rhodobacter capsulatus
1.3.1.75 Strep-Tactin Sepharose column chromatography and Sephacryl S-200 gel filtration Rhodobacter capsulatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+
-
 Rhodobacter capsulatus chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+
-
 Rhodobacter capsulatus NBRC 16581 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+
-
 Rhodobacter capsulatus ATCC BAA-309 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+
-
 Rhodobacter capsulatus SB1003 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+
-
 Rhodobacter capsulatus protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+
-
 Rhodobacter capsulatus NBRC 16581 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+
-
 Rhodobacter capsulatus ATCC BAA-309 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+
-
 Rhodobacter capsulatus SB1003 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 additional information measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction Rhodobacter capsulatus ?
-
-
1.3.1.75 additional information measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction Rhodobacter capsulatus NBRC 16581 ?
-
-
1.3.1.75 additional information measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction Rhodobacter capsulatus ATCC BAA-309 ?
-
-
1.3.1.75 additional information measurement of the absorbance decrease at around 340 nm attributable to the consumption of NADPH by the enzymatic reaction Rhodobacter capsulatus SB1003 ?
-
-
1.3.7.15 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
-
 ?
1.3.7.15 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
-
 ?
1.3.7.15 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
-
 ?
1.3.7.15 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
-
 ?
1.3.7.15 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Rhodobacter capsulatus chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.7.15 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Rhodobacter capsulatus NBRC 16581 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.7.15 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
-
 ?
1.3.7.15 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Rhodobacter capsulatus SB1003 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.75 ? x * 35000, Strep-tag II-tagged enzyme, SDS-PAGE Rhodobacter capsulatus
1.3.1.75 ? x * 35900, Strep-tag II-tagged enzyme, calculated from amino acid sequence Rhodobacter capsulatus
1.3.1.75 More BciA forms a functional oligomeric complex consisting of at least three rigid dimers. BciA requires NADPH as an electron donor for its C8-vinyl reduction activity. The BciA oligomer shows 90fold higher kcat values compared to the dimer. On the other hand, the dimer shows the similar kcat values both on the high and low NaCl concentrations. These suggests that disassembly of the oligomer to the dimer induces a structural change around the catalytic site of the enzyme, thereby decreasing the enzymatic activity of the dimer. In contrast, the Km value for the oligomer is comparable to that for the dimer, suggesting that the affinity of BciA for the substrate DV-Chlide a is retained following disassembly of the oligomer to the dimer. The oligomerization of BciA does not cause any allosteric effect on binding of DV-Chlide a at the catalytic center Rhodobacter capsulatus
1.3.1.75 oligomer x * 35900, recombinant N-terminally Strep II-tagged enzyme BciA, SDS-PAGE Rhodobacter capsulatus
1.3.7.15 More one BchYZ heterodimer is assumed as a minimal active protomer Rhodobacter capsulatus

Synonyms

EC Number Synonyms Comment Organism
1.3.1.75 BciA
-
 Rhodobacter capsulatus
1.3.1.75 C8-vinyl reductase
-
 Rhodobacter capsulatus
1.3.1.75 NADPH-dependent divinyl reductase
-
 Rhodobacter capsulatus
1.3.7.15 a-COR
-
 Rhodobacter capsulatus
1.3.7.15 BchX
-
 Rhodobacter capsulatus
1.3.7.15 BchY
-
 Rhodobacter capsulatus
1.3.7.15 BchZ
-
 Rhodobacter capsulatus
1.3.7.15 COR
-
 Rhodobacter capsulatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.1.75 22
-
 assay at room temperature Rhodobacter capsulatus
1.3.7.15 22
-
 assay at room temperature Rhodobacter capsulatus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.75 0.0071
-
 3,8-divinyl chlorophyllide a pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, low salt condition Rhodobacter capsulatus
1.3.1.75 0.0071
-
 3,8-divinyl protochlorophyllide a dimeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C Rhodobacter capsulatus
1.3.1.75 0.0074
-
 3,8-divinyl chlorophyllide a pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, high salt condition Rhodobacter capsulatus
1.3.1.75 0.0074
-
 3,8-divinyl protochlorophyllide a dimeric enzyme (high salt condition, 1 M NaCl), at pH 8.0 and 25°C Rhodobacter capsulatus
1.3.1.75 0.66
-
 3,8-divinyl chlorophyllide a pH 8.0, 22°C, recombinant Strep II-tagged oligomeric enzyme, low salt condition Rhodobacter capsulatus
1.3.1.75 0.66
-
 3,8-divinyl protochlorophyllide a oligomeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C Rhodobacter capsulatus
1.3.7.15 0.011
-
 8-vinyl chlorophyllide a pH 8.0, 22°C, recombinant BchYZ heterodimer Rhodobacter capsulatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.75 8
-
 assay at Rhodobacter capsulatus
1.3.7.15 8
-
 assay at Rhodobacter capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.75 NADPH dependent on Rhodobacter capsulatus
1.3.7.15 FAD
-
 Rhodobacter capsulatus
1.3.7.15 Fe-S center
-
 Rhodobacter capsulatus
1.3.7.15 Ferredoxin
-
 Rhodobacter capsulatus

General Information

EC Number General Information Comment Organism
1.3.1.75 evolution BciA (NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR, EC 1.3.7.15). 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 from Rhodobacter capsulatus, BciA has a lower affinity for DV-Chlide a but a much higher specific activity Rhodobacter capsulatus
1.3.1.75 physiological function BciA is a plant-type NADPH-dependent divinyl reductase, it works for 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
1.3.7.15 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
1.3.7.15 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.3.1.75 0.21
-
 3,8-divinyl protochlorophyllide a dimeric enzyme (high salt condition, 1 M NaCl), at pH 8.0 and 25°C Rhodobacter capsulatus
1.3.1.75 0.211
-
 3,8-divinyl chlorophyllide a pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, high salt condition Rhodobacter capsulatus
1.3.1.75 0.22
-
 3,8-divinyl protochlorophyllide a dimeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C Rhodobacter capsulatus
1.3.1.75 0.222
-
 3,8-divinyl chlorophyllide a pH 8.0, 22°C, recombinant Strep II-tagged dimeric enzyme, low salt condition Rhodobacter capsulatus
1.3.1.75 28.7
-
 3,8-divinyl chlorophyllide a pH 8.0, 22°C, recombinant Strep II-tagged oligomeric enzyme, low salt condition Rhodobacter capsulatus
1.3.1.75 29
-
 3,8-divinyl protochlorophyllide a oligomeric enzyme (low salt condition, 150 mM NaCl), at pH 8.0 and 25°C Rhodobacter capsulatus
1.3.7.15 1.864
-
 8-vinyl chlorophyllide a pH 8.0, 22°C, recombinant BchYZ heterodimer Rhodobacter capsulatus