BRENDA - Enzyme Database
show all sequences of 1.3.1.75

Isolation and structural determination of C8-vinyl-bacteriochlorophyll d from the bciA and bchU double mutant of the green sulfur bacterium Chlorobaculum tepidum

Harada, J.; Mizoguchi, T.; Nomura, K.; Tamiaki, H.; Photosyn. Res. 121, 13-23 (2014)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
construction of mutant tepdA lacking enzymes BciA and BchU, that catalyze reduction of the C8-vinyl group and methylation at the C20 position of bacteriochlorophyll (BChl) c, respectively, in the green sulfur bacterium Chlorobaculum tepidum, the mutant accumula C8-vinyl-bacteriochlorophyllide d derivative, determined by NMR to be (31R)-8-vinyl-12-ethyl-(R[V,E])BChl d. The bciA mutant possesses mainly (31R)-8-vinyl-12-ethyl-(R[V,E])BChl c as in chlorosomal self-aggregates in addition to minor (31R)-8-vinyl-12-methyl-(R[V,M]) and (31S)-8-vinyl-12-ethyl-(S[V,E])BChls c. Reconstitution of self-aggregates of C8V-BChl species in vitro. Comparison of chlorophyllide a derivatives in tepdA strains lacking bciA and/or bciU, overview
Chlorobaculum tepidum
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
Chlorobaculum tepidum
-
bacteriochlorophyllide a + NADP+
-
-
-
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
Chlorobaculum tepidum TLS
-
bacteriochlorophyllide a + NADP+
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chlorobaculum tepidum
Q8KDI7
-
-
Chlorobaculum tepidum TLS
Q8KDI7
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
-
745981
Chlorobaculum tepidum
bacteriochlorophyllide a + NADP+
-
-
-
-
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
-
745981
Chlorobaculum tepidum TLS
bacteriochlorophyllide a + NADP+
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
-
Chlorobaculum tepidum
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
-
Chlorobaculum tepidum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
construction of mutant tepdA lacking enzymes BciA and BchU, that catalyze reduction of the C8-vinyl group and methylation at the C20 position of bacteriochlorophyll (BChl) c, respectively, in the green sulfur bacterium Chlorobaculum tepidum, the mutant accumula C8-vinyl-bacteriochlorophyllide d derivative, determined by NMR to be (31R)-8-vinyl-12-ethyl-(R[V,E])BChl d. The bciA mutant possesses mainly (31R)-8-vinyl-12-ethyl-(R[V,E])BChl c as in chlorosomal self-aggregates in addition to minor (31R)-8-vinyl-12-methyl-(R[V,M]) and (31S)-8-vinyl-12-ethyl-(S[V,E])BChls c. Reconstitution of self-aggregates of C8V-BChl species in vitro. Comparison of chlorophyllide a derivatives in tepdA strains lacking bciA and/or bciU, overview
Chlorobaculum tepidum
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
Chlorobaculum tepidum
-
bacteriochlorophyllide a + NADP+
-
-
-
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
Chlorobaculum tepidum TLS
-
bacteriochlorophyllide a + NADP+
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
-
745981
Chlorobaculum tepidum
bacteriochlorophyllide a + NADP+
-
-
-
-
3,8-divinyl bacteriochlorophyllide a + NADPH + H+
-
745981
Chlorobaculum tepidum TLS
bacteriochlorophyllide a + NADP+
-
-
-
-
General Information
General Information
Commentary
Organism
malfunction
the bciA deletion mutant of Chlorobaculum tepidum accumulates C8V pigments. The bciA mutant possesses mainly (31R)-8-vinyl-12-ethyl-(R[V,E])BChl c as in chlorosomal self-aggregates in addition to minor (31R)-8-vinyl-12-methyl-(R[V,M]) and (31S)-8-vinyl-12-ethyl-(S[V,E])BChls c
Chlorobaculum tepidum
General Information (protein specific)
General Information
Commentary
Organism
malfunction
the bciA deletion mutant of Chlorobaculum tepidum accumulates C8V pigments. The bciA mutant possesses mainly (31R)-8-vinyl-12-ethyl-(R[V,E])BChl c as in chlorosomal self-aggregates in addition to minor (31R)-8-vinyl-12-methyl-(R[V,M]) and (31S)-8-vinyl-12-ethyl-(S[V,E])BChls c
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)
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Isolation and structural dete ...
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746037
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