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Literature summary extracted from

  • Yamamoto, H.; Mizoguchi, T.; Tsukatani, Y.; Tamiaki, H.; Kurisu, G.; Fujita, Y.
    Chlorophyllide a oxidoreductase preferentially catalyzes 8-vinyl reduction over B-ring reduction of 8-vinyl chlorophyllide a in the late steps of bacteriochlorophyll biosynthesis (2020), ChemBioChem, 21, 1760-1766 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.7.15 genes bchX and bchY, recombinant expression of GST-tagged BchX and BchY in Escherichia coli Rhodobacter capsulatus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.7.15 8-vinyl chlorophyllide a inhibitory effect of 8 V-Chlide on 3 V-BChlide production inhibitory effect of 8 V-Chlide on the C7=C8 reduction of COR Rhodobacter capsulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.75 0.23
-
 8-vinyl chlorophyllide a pH and temperature not specified in the publication Rhodobacter capsulatus
1.3.7.15 0.0014
-
 8-vinyl chlorophyllide a recombinant enzyme BchX/BchY, pH and temperature not specified in the publication Rhodobacter capsulatus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.7.15 Mg2+ required 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+ Chlorobaculum tepidum preferred substrate chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ Chlorobaculum tepidum ATCC 49652 preferred substrate chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ Chlorobaculum tepidum TLS0 preferred substrate chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ Chlorobaculum tepidum DSM 12025 preferred substrate chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ Chlorobaculum tepidum NBRC 103806 preferred substrate chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+ Chlorobaculum tepidum
-
 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+ Chlorobaculum tepidum ATCC 49652
-
 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+ Chlorobaculum tepidum TLS0
-
 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+ Chlorobaculum tepidum DSM 12025
-
 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+ Chlorobaculum tepidum NBRC 103806
-
 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 8-vinyl chlorophyllide a + NADPH + H+ Rhodobacter capsulatus preferred reaction of BciA chlorophyllide a + NADP+
-
 ?
1.3.7.13 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster Chloroherpeton thalassium
-
 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 ?
1.3.7.13 protochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster Chloroherpeton thalassium
-
 8-vinyl protochlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 ?
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 Chlorobaculum tepidum Q8KDI7 Chlorobium tepidum
-
1.3.1.75 Chlorobaculum tepidum ATCC 49652 Q8KDI7 Chlorobium tepidum
-
1.3.1.75 Chlorobaculum tepidum DSM 12025 Q8KDI7 Chlorobium tepidum
-
1.3.1.75 Chlorobaculum tepidum NBRC 103806 Q8KDI7 Chlorobium tepidum
-
1.3.1.75 Chlorobaculum tepidum TLS0 Q8KDI7 Chlorobium tepidum
-
1.3.1.75 Rhodobacter capsulatus
-
-
-
1.3.7.13 Chloroherpeton thalassium
-
-
-
1.3.7.15 Rhodobacter capsulatus P26177 gene bchX
-
1.3.7.15 Rhodobacter capsulatus ATCC BAA-309 P26177 gene bchX
-
1.3.7.15 Rhodobacter capsulatus NBRC 16581 P26177 gene bchX
-
1.3.7.15 Rhodobacter capsulatus SB1003 P26177 gene bchX
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.7.15 copurification of recombinant GST-tagged BchX and BchY from Escherichia coli by glutathione affinity chromatography Rhodobacter capsulatus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.75 1.1
-
 recombinant BciA, pH and temperature not specified in the publication Chlorobaculum tepidum

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+
-
 Chlorobaculum tepidum chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ preferred substrate Chlorobaculum tepidum chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+
-
 Chlorobaculum tepidum ATCC 49652 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ preferred substrate Chlorobaculum tepidum ATCC 49652 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+
-
 Chlorobaculum tepidum TLS0 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ preferred substrate Chlorobaculum tepidum TLS0 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+
-
 Chlorobaculum tepidum DSM 12025 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ preferred substrate Chlorobaculum tepidum DSM 12025 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+
-
 Chlorobaculum tepidum NBRC 103806 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + NADPH + H+ preferred substrate Chlorobaculum tepidum NBRC 103806 chlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+
-
 Chlorobaculum tepidum protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+
-
 Chlorobaculum tepidum ATCC 49652 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+
-
 Chlorobaculum tepidum TLS0 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+
-
 Chlorobaculum tepidum DSM 12025 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + NADPH + H+
-
 Chlorobaculum tepidum NBRC 103806 protochlorophyllide a + NADP+
-
 ?
1.3.1.75 8-vinyl chlorophyllide a + NADPH + H+ preferred reaction of BciA Rhodobacter capsulatus chlorophyllide a + NADP+
-
 ?
1.3.7.13 chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 Chloroherpeton thalassium 8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 ?
1.3.7.13 protochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
 Chloroherpeton thalassium 8-vinyl protochlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 ?
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
-
 ?
1.3.7.15 additional information enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75 Rhodobacter capsulatus ?
-
-
1.3.7.15 additional information enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75 Rhodobacter capsulatus NBRC 16581 ?
-
-
1.3.7.15 additional information enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75 Rhodobacter capsulatus ATCC BAA-309 ?
-
-
1.3.7.15 additional information enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75 Rhodobacter capsulatus SB1003 ?
-
-

Subunits

EC Number Subunits Comment Organism
1.3.7.15 More In contrast to BciA and BciB, COR is a nitrogenase-like complex enzyme consisting of two separable components, the X protein (a BchX dimer) and the YZ protein (a BchY-BchZ heterotetramer). The X protein serves as the reductase component by transferring electrons from a [4Fe-4S] cluster held in the interface between the BchX homodimer to the YZ protein. The YZ protein is the catalytic component, as it accepts electrons from the X protein and transfers them to the Chlide substrate via a [4Fe-4S] cluster, to produce 3-vinyl bacteriochlorophyllide a (3 V-BChlide) Rhodobacter capsulatus

Synonyms

EC Number Synonyms Comment Organism
1.3.1.75 8VR
-
 Chlorobaculum tepidum
1.3.1.75 BciA
-
 Rhodobacter capsulatus
1.3.1.75 BciA
-
 Chlorobaculum tepidum
1.3.1.75 C8 vinyl reductase
-
 Rhodobacter capsulatus
1.3.1.75 C8 vinyl reductase
-
 Chlorobaculum tepidum
1.3.1.75 cvrA
-
 Chlorobaculum tepidum
1.3.1.75 divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic UniProt Chlorobaculum tepidum
1.3.1.75 NADPH-dependent 8VR
-
 Rhodobacter capsulatus
1.3.7.13 8VR
-
 Chloroherpeton thalassium
1.3.7.13 bciB
-
 Chloroherpeton thalassium
1.3.7.13 C8 vinyl reductase
-
 Chloroherpeton thalassium
1.3.7.13 cvrA
-
 Chloroherpeton thalassium
1.3.7.15 chlorophyllide a oxidoreductase
-
 Rhodobacter capsulatus
1.3.7.15 COR
-
 Rhodobacter capsulatus
1.3.7.15 COR 8VR
-
 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 0.66
-
 8-vinyl chlorophyllide a pH and temperature not specified in the publication Rhodobacter capsulatus
1.3.1.75 0.66
-
 3,8-divinyl chlorophyllide a recombinant BciA, pH and temperature not specified in the publication Chlorobaculum tepidum
1.3.7.15 0.00027
-
 8-vinyl chlorophyllide a recombinant enzyme BchX/BchY, pH and temperature not specified in the publication Rhodobacter capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.75 NADPH
-
 Chlorobaculum tepidum
1.3.7.13 FAD
-
 Chloroherpeton thalassium
1.3.7.13 Fe-S center
-
 Chloroherpeton thalassium
1.3.7.13 Ferredoxin
-
 Chloroherpeton thalassium
1.3.7.15 ATP
-
 Rhodobacter capsulatus
1.3.7.15 Fe-S center a [4Fe-4S] cluster is bound at the interface between the BchX homodimer and the YZ protein of the COR enzyme complex Rhodobacter capsulatus
1.3.7.15 Ferredoxin
-
 Rhodobacter capsulatus

General Information

EC Number General Information Comment Organism
1.3.1.75 metabolism bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR, EC 1.3.7.15), respectively, to produce 3-vinyl-bacteriochlorphyllide a Chlorobaculum tepidum
1.3.1.75 physiological function bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH. BciA is an NADPH-dependent 8VR with a preference for the 8-vinyl chlorophyllide a (8 V-Chlide) substrate compared with 8-vinyl PChlide (8 V-PChlide) Chlorobaculum tepidum
1.3.7.13 metabolism bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR, EC 1.3.7.15), respectively, to produce 3-vinyl-bacteriochlorphyllide a Chloroherpeton thalassium
1.3.7.13 physiological function bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB, and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide Chloroherpeton thalassium
1.3.7.15 metabolism bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH Rhodobacter capsulatus
1.3.7.15 physiological function bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. The COR activity can act as a third 8VR, confirmed in vivo by the loss of 8VR activity mutants lacking bciA and genes encoding subunits of COR. In contrast to BciA and BciB, COR is a nitrogenase-like complex enzyme consisting of two separable components, the X protein (a BchX dimer) and the YZ protein (a BchY-BchZ heterotetramer). The X protein serves as the reductase component by transferring electrons from a [4Fe-4S] cluster held in the interface between the BchX homodimer and the YZ protein. The YZ protein is the catalytic component, as it accepts electrons from the X protein and transfers them to the Chlide substrate via a [4Fe-4S] cluster, to produce 3-vinyl bacteriochlorophyllide a (3 V-BChlide). 3 V-BChlide is produced via Chlide rather than via 3,8-divinyl BChlide (81,82-didehydro-3 V-BChlide) Rhodobacter capsulatus