BRENDA - Enzyme Database
show all sequences of 1.3.1.111

Rhodospirillum rubrum possesses a variant of the bchP gene, encoding geranylgeranyl-bacteriopheophytin reductase

Addlesee, H.A.; Hunter, C.N.; J. Bacteriol. 184, 1578-1586 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene bchP, DNA and amino acid sequence determination and analysis, sequence comparison
Rhodospirillum rubrum
Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of a a hybrid gene consisting of the 5'half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
Rhodobacter sphaeroides
additional information
construction of a hybrid gene consisting of the 5' half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
Rhodospirillum rubrum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
bacteriochlorophyll a + 3 NADP+
Rhodobacter sphaeroides
-
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
?
bacteriopheophytin a + 3 NADP+
Rhodospirillum rubrum
-
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
-
-
?
bacteriopheophytin a + 3 NADP+
Rhodobacter sphaeroides
-
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodobacter sphaeroides
Q9Z5D4
; gene bchP
-
Rhodospirillum rubrum
Q936J5
; gene bchP
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
bacteriochlorophyll a + 3 NADP+
-
692822
Rhodobacter sphaeroides
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
-
?
bacteriopheophytin a + 3 NADP+
-
692822
Rhodospirillum rubrum
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
-
-
-
?
bacteriopheophytin a + 3 NADP+
-
692822
Rhodobacter sphaeroides
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
-
-
-
?
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
-
692822
Rhodospirillum rubrum
phytyl-bacteriochlorophyll a + 3 NADP+
-
-
-
?
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
-
692822
Rhodobacter sphaeroides
phytyl-bacteriochlorophyll a + 3 NADP+
-
-
-
?
geranylgeranyl-bacteriopheophytin a + NADPH + H+
-
692822
Rhodobacter sphaeroides
phytyl-bacteriopheophytin a + NADP+
-
-
-
?
additional information
no activity with geranylgeranyl-bacteriopheophytin a
692822
Rhodospirillum rubrum
?
-
-
-
-
additional information
no activity with bacteriochlorophyll a
692822
Rhodospirillum rubrum
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Rhodospirillum rubrum
NADP+
-
Rhodobacter sphaeroides
NADPH
-
Rhodobacter sphaeroides
NADPH
-
Rhodospirillum rubrum
Cloned(Commentary) (protein specific)
Commentary
Organism
gene bchP, DNA and amino acid sequence determination and analysis, sequence comparison
Rhodospirillum rubrum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Rhodospirillum rubrum
NADP+
-
Rhodobacter sphaeroides
NADPH
-
Rhodobacter sphaeroides
NADPH
-
Rhodospirillum rubrum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of a a hybrid gene consisting of the 5'half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
Rhodobacter sphaeroides
additional information
construction of a hybrid gene consisting of the 5' half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
Rhodospirillum rubrum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
bacteriochlorophyll a + 3 NADP+
Rhodobacter sphaeroides
-
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
?
bacteriopheophytin a + 3 NADP+
Rhodospirillum rubrum
-
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
-
-
?
bacteriopheophytin a + 3 NADP+
Rhodobacter sphaeroides
-
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
bacteriochlorophyll a + 3 NADP+
-
692822
Rhodobacter sphaeroides
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
-
?
bacteriopheophytin a + 3 NADP+
-
692822
Rhodospirillum rubrum
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
-
-
-
?
bacteriopheophytin a + 3 NADP+
-
692822
Rhodobacter sphaeroides
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
-
-
-
?
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
-
692822
Rhodospirillum rubrum
phytyl-bacteriochlorophyll a + 3 NADP+
-
-
-
?
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
-
692822
Rhodobacter sphaeroides
phytyl-bacteriochlorophyll a + 3 NADP+
-
-
-
?
geranylgeranyl-bacteriopheophytin a + NADPH + H+
-
692822
Rhodobacter sphaeroides
phytyl-bacteriopheophytin a + NADP+
-
-
-
?
additional information
no activity with geranylgeranyl-bacteriopheophytin a
692822
Rhodospirillum rubrum
?
-
-
-
-
additional information
no activity with bacteriochlorophyll a
692822
Rhodospirillum rubrum
?
-
-
-
-
General Information
General Information
Commentary
Organism
malfunction
the enzyme only catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin. It might be a naturally occurring bchP mutant with an insertion mutation that may have been the initial cause of a partial loss of function
Rhodospirillum rubrum
metabolism
requirement of Rhodospirillum rubrum for phytylated bacteriopheophytin, a potential link between the absence of light-harvesting complex 2 and of phytylated bacteriochlorophyll from the wild-type bacterium. In addition to bacteriochlorophyll, the reaction center of purple bacteria contains two bacteriopheophytin molecules, one of which is the first clearly resolved acceptor of electrons, following electron transfer from the bacteriochlorophyll dimer. Proposed pathway for reduction of geranylgeranyl bacteriopheophytin a in Rhodospirillum rubrum, reduction proceeds via dihydro-GG-esterified and tetrahydro-GG-esterified intermediates to the final product, phytylated bacteriopheophytin
Rhodospirillum rubrum
physiological function
the enzyme is responsible for the reduction of the isoprenoid moiety of bacteriochlorophyll (Bchl) from geranylgeraniol (GG) to phytol, it also catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin
Rhodobacter sphaeroides
General Information (protein specific)
General Information
Commentary
Organism
malfunction
the enzyme only catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin. It might be a naturally occurring bchP mutant with an insertion mutation that may have been the initial cause of a partial loss of function
Rhodospirillum rubrum
metabolism
requirement of Rhodospirillum rubrum for phytylated bacteriopheophytin, a potential link between the absence of light-harvesting complex 2 and of phytylated bacteriochlorophyll from the wild-type bacterium. In addition to bacteriochlorophyll, the reaction center of purple bacteria contains two bacteriopheophytin molecules, one of which is the first clearly resolved acceptor of electrons, following electron transfer from the bacteriochlorophyll dimer. Proposed pathway for reduction of geranylgeranyl bacteriopheophytin a in Rhodospirillum rubrum, reduction proceeds via dihydro-GG-esterified and tetrahydro-GG-esterified intermediates to the final product, phytylated bacteriopheophytin
Rhodospirillum rubrum
physiological function
the enzyme is responsible for the reduction of the isoprenoid moiety of bacteriochlorophyll (Bchl) from geranylgeraniol (GG) to phytol, it also catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin
Rhodobacter sphaeroides
Other publictions for EC 1.3.1.111
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)
736948
Harada
Accumulation of chlorophyllous ...
Chlorobaculum tepidum, Chlorobaculum tepidum WT2321
Photochem. Photobiol. Sci.
7
1179-1187
2008
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2
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1
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2
2
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-
692822
Addlesee
Rhodospirillum rubrum possesse ...
Rhodobacter sphaeroides, Rhodospirillum rubrum
J. Bacteriol.
184
1578-1586
2002
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1
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2
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3
-
6
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8
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4
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1
4
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8
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3
3
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-
692821
Addlesee
Physical mapping and functiona ...
Rhodobacter sphaeroides
J. Bacteriol.
181
7248-7255
1999
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1
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1
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4
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1
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1
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4
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1
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1
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3
3
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-
736098
Addlesee
Cloning, sequencing and functi ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides NCIB 8253, Synechocystis sp.
FEBS Lett.
389
126-130
1996
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2
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1
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1
3
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3
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3
1
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2
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1
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3
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3
1
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3
3
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735661
Bollivar
Molecular genetic analysis of ...
Rhodobacter capsulatus, Rhodobacter capsulatus SB1003
Biochemistry
33
12763-12768
1994
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1
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1
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1
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1
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4
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2
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