BRENDA - Enzyme Database
show all sequences of 1.3.1.75

A tale of two reductases extending the bacteriochlorophyll biosynthetic pathway in E. coli

Tikh, I.B.; Quin, M.B.; Schmidt-Dannert, C.; PLoS ONE 9, e89734 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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
Rhodobacter sphaeroides
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
Engineering
Amino acid exchange
Commentary
Organism
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
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
Rhodobacter sphaeroides
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
Rhodobacter sphaeroides
-
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
Chlorobaculum tepidum
-
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
Chlorobaculum tepidum TLS
-
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
Rhodobacter sphaeroides
-
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chlorobaculum tepidum
Q8KDI7
-
-
Chlorobaculum tepidum TLS
Q8KDI7
-
-
Rhodobacter sphaeroides
Q3IXP7
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Chlorobaculum tepidum
recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Rhodobacter sphaeroides
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
746260
Rhodobacter sphaeroides
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
746260
Chlorobaculum tepidum
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
746260
Chlorobaculum tepidum TLS
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
746260
Rhodobacter sphaeroides
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
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
746260
Chlorobaculum tepidum
?
-
-
-
-
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
746260
Rhodobacter sphaeroides
?
-
-
-
-
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
746260
Chlorobaculum tepidum TLS
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Chlorobaculum tepidum
37
-
assay at
Rhodobacter sphaeroides
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Chlorobaculum tepidum
8
-
assay at
Rhodobacter sphaeroides
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
NADPH-dependent, the enzyme sequence contains the conserved GxxGxxG motif, required for NAD(P)H binding
Chlorobaculum tepidum
NADPH
NADPH-dependent, the enzyme sequence contains the conserved GxxGxxG motif, required for NAD(P)H binding
Rhodobacter sphaeroides
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Rhodobacter sphaeroides
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
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
NADPH-dependent, the enzyme sequence contains the conserved GxxGxxG motif, required for NAD(P)H binding
Chlorobaculum tepidum
NADPH
NADPH-dependent, the enzyme sequence contains the conserved GxxGxxG motif, required for NAD(P)H binding
Rhodobacter sphaeroides
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
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
Rhodobacter sphaeroides
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
Rhodobacter sphaeroides
-
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
Chlorobaculum tepidum
-
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
Chlorobaculum tepidum TLS
-
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
Rhodobacter sphaeroides
-
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Chlorobaculum tepidum
recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Rhodobacter sphaeroides
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
746260
Rhodobacter sphaeroides
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
746260
Chlorobaculum tepidum
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
746260
Chlorobaculum tepidum TLS
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
746260
Rhodobacter sphaeroides
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
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
746260
Chlorobaculum tepidum
?
-
-
-
-
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
746260
Rhodobacter sphaeroides
?
-
-
-
-
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
746260
Chlorobaculum tepidum TLS
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Chlorobaculum tepidum
37
-
assay at
Rhodobacter sphaeroides
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Chlorobaculum tepidum
8
-
assay at
Rhodobacter sphaeroides
General Information
General Information
Commentary
Organism
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
General Information (protein specific)
General Information
Commentary
Organism
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
Other publictions for EC 1.3.1.75
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745221
Chen
Two unrelated 8-vinyl reducta ...
Acaryochloris marina, Acaryochloris marina MBIC11017
J. Bacteriol.
198
1393-1400
2016
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4
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746442
Tsukatani
Rhodobacter sphaeroides mutan ...
Rhodobacter sphaeroides
Sci. Rep.
5
9741
2015
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1
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5
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1
1
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736444
Harada
Chlorophyllide a oxidoreductas ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides J001, Rhodopseudomonas palustris, Rhodopseudomonas palustris J002
J. Biol. Chem.
289
12716-12726
2014
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2
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5
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7
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5
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4
4
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744270
Canniffe
Elucidation of the preferred ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides DSM 158
Biochem. J.
462
433-440
2014
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2
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1
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745981
Harada
Isolation and structural dete ...
Chlorobaculum tepidum, Chlorobaculum tepidum TLS
Photosyn. Res.
121
13-23
2014
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746037
Ito
Evolution of a new chlorophyl ...
Arabidopsis thaliana, Phaeodactylum tricornutum
Plant Cell Physiol.
55
593-603
2014
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2
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4
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746260
Tikh
A tale of two reductases exte ...
Chlorobaculum tepidum, Chlorobaculum tepidum TLS, Rhodobacter sphaeroides
PLoS ONE
9
e89734
2014
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1
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746105
Wang
One divinyl reductase reduces ...
Arabidopsis thaliana, Cucumis sativus, Oryza sativa, Zea mays
Plant Physiol.
161
521-534
2013
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4
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1
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9
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726217
Wang
Divinyl chlorophyll(ide) a can ...
Oryza sativa
Plant Physiol.
153
994-1003
2010
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739277
Nagata
The major route for chlorophyl ...
Arabidopsis thaliana
Plant Cell Physiol.
48
1803-1808
2007
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667191
Kolossov
Chloroplast biogenesis 92: In ...
Cucumis sativus
Anal. Biochem.
348
192-197
2006
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639381
Kolossov
Chloroplast biogenesis 84: sol ...
Cucumis sativus, Hordeum vulgare
Anal. Biochem.
295
214-219
2001
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2
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1
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7
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2
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1
4
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1
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1
1
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3
1
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9
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6
1
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5
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1
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3
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4
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4
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