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Literature summary extracted from

  • Tikh, I.B.; Quin, M.B.; Schmidt-Dannert, C.
    A tale of two reductases extending the bacteriochlorophyll biosynthetic pathway in E. coli (2014), PLoS ONE, 9, e89734 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.75 gene bciA, recombinant expression in Escherichia coli strain BL21(DE3), coexpression with the enzymes of the biosynthetic pathway, engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli, overview. RSBciA is active, albeit not in vivo with the engineered pathway. Subcloning in Escherichia coli strain JM109 Cereibacter sphaeroides
1.3.1.75 gene bciA, recombinant expression in Escherichia coli, coexpression with the enzymes of the biosynthetic pathway, engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli, overview. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway. Subcloning in Escherichia coli strain JM109 Chlorobaculum tepidum

Protein Variants

EC Number Protein Variants Comment Organism
1.3.1.75 additional information engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli expressing the enzyme involved originating from different organisms, overview. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway. No mono-vinyl forms of any of the pathway intermediates upon coexpression of the 8-vinyl reductase with BchSID and BchM. PIX overproducing cells expressing BchSID and CTBciA alone produce two additional compounds, mono-vinyl PIX (mvPIX) and mono-vinyl MgPIX (mvMgPIX), indicating that CTBciA is capable of reducing the C8-vinyl group on both the Mg chelated and the non-Mg chelated porphyrin molecule Chlorobaculum tepidum
1.3.1.75 additional information engineered pathway design for the heterologous production of bacteriochlorophyll in the non-photosynthetic host Escherichia coli expressing the enzyme involved originating from different organisms, overview. RSBciA is completely inactive in our recombinant system. RSBciA is completely inactive in our recombinant system. Subcloning in Escherichia coli strain JM109 Cereibacter sphaeroides

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 + reduced ferredoxin [iron-sulfur] cluster + H+ Cereibacter sphaeroides
-
 chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ Chlorobaculum tepidum
-
 chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ Chlorobaculum tepidum TLS
-
 chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ Cereibacter sphaeroides
-
 protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.75 Cereibacter sphaeroides Q3IXP7
-
-
1.3.1.75 Chlorobaculum tepidum Q8KDI7
-
-
1.3.1.75 Chlorobaculum tepidum TLS Q8KDI7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.75 recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Cereibacter sphaeroides
1.3.1.75 recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography 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 + reduced ferredoxin [iron-sulfur] cluster + H+
-
 Cereibacter sphaeroides chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
 Chlorobaculum tepidum chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.1.75 3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
 Chlorobaculum tepidum TLS chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.1.75 3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
 Cereibacter sphaeroides protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
 ?
1.3.1.75 additional information the 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway Chlorobaculum tepidum ?
-
 ?
1.3.1.75 additional information the native 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. Recombinant enzyme RSBciA is active, albeit not in vivo with the engineered pathway, but shows very slow activity Cereibacter sphaeroides ?
-
 ?
1.3.1.75 additional information the 8-vinyl reductase is substrate promiscuous, capable of reducing the C8-vinyl group of Mg protoporphyrin IX, Mg protoporphyrin IX methylester, and divinyl protochlorophyllide. The enzyme activity is dependent upon the presence of chelated Mg2+ in the porphyrin ring, with no activity against non-Mg2+ chelated intermediates observed. CTBciA is capable of reducing the C8-vinyl group of several different intermediates in the BChl pathway Chlorobaculum tepidum TLS ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.1.75 8-vinyl reductase
-
 Cereibacter sphaeroides
1.3.1.75 8-vinyl reductase
-
 Chlorobaculum tepidum
1.3.1.75 BciA
-
 Cereibacter sphaeroides
1.3.1.75 BciA
-
 Chlorobaculum tepidum
1.3.1.75 CTBciA
-
 Chlorobaculum tepidum
1.3.1.75 ct_1063
-
 Chlorobaculum tepidum
1.3.1.75 NADPH-dependent reductase BciA
-
 Cereibacter sphaeroides
1.3.1.75 NADPH-dependent reductase BciA
-
 Chlorobaculum tepidum
1.3.1.75 RSBciA
-
 Cereibacter sphaeroides
1.3.1.75 RSP_3070
-
 Cereibacter sphaeroides

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.1.75 37
-
 assay at Cereibacter sphaeroides
1.3.1.75 37
-
 assay at Chlorobaculum tepidum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.75 8
-
 assay at Cereibacter sphaeroides
1.3.1.75 8
-
 assay at Chlorobaculum tepidum

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.75 NADPH NADPH-dependent, the enzyme sequence contains the conserved GxxGxxG motif, required for NAD(P)H binding Cereibacter sphaeroides
1.3.1.75 NADPH NADPH-dependent, the enzyme sequence contains the conserved GxxGxxG motif, required for NAD(P)H binding Chlorobaculum tepidum

General Information

EC Number General Information Comment Organism
1.3.1.75 metabolism green bacteria like Chlorobaculum tepidum are unique in that they are able to produce different types of Chls and Bchls, and encode in their genomes several homologs (BchS, T) of the large subunit (BchH) of the magnesium chelatase, which may play a role in regulating the types of (B)Chls produced Chlorobaculum tepidum