BRENDA - Enzyme Database show
show all sequences of 2.1.1.11

Characterization of three homologs of the large subunit of the magnesium chelatase from Chlorobaculum tepidum and interaction with the magnesium protoporphyrin IX methyltransferase

Johnson, E.T.; Schmidt-Dannert, C.; J. Biol. Chem. 283, 27776-27784 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli JM109, constitutive promoter on pUCmod, overexpression improved by using BL21 cells in combination with T7 promoter, subclconing into pET-20b(+) vector, engineered Escherichia coli strain overproducing protoporphyrin for activity assays
Chlorobaculum tepidum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0006
-
magnesium protoporphyrin
concentrations between 0.3 and 30 microM in the presence of 50 nM enzyme
Chlorobaculum tepidum
0.053
-
protoporphyrin
concentrations between 1 and 30 microM in the presence of 200 nM enzyme
Chlorobaculum tepidum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chlorobaculum tepidum
-
formerly Chlorobium tepidum
-
Purification (Commentary)
Commentary
Organism
recombinant protein, gel filtration and SDS-PAGE
Chlorobaculum tepidum
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell culture
-
Chlorobaculum tepidum
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
activity assay in protoporphyrin overproducing Escherichia coli cells, interaction of subunits of the three magnesium chelatase complexes with magnesium protoporphyrin methyltransferase, differences in subunit interactions either increase or decrease methyltransferase activity, vice versa, activity of any of the three magnesium chelatase complexes not affected
Chlorobaculum tepidum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + magnesium protoporphyrin
different substrate specificity, protoporphyrin with or without bound metal as a substrate
687761
Chlorobaculum tepidum
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + protoporphyrin
methyl transfer possible without bound metal, slow reaction rate
687761
Chlorobaculum tepidum
S-adenosyl-L-homocysteine + protoporphyrin monomethyl ester
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
majority of the protein exist as a high-molecular-weight multimer as determined by gel filtration
Chlorobaculum tepidum
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Chlorobaculum tepidum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0002
-
protoporphyrin
concentrations between 1 and 30 microM in the presence of 200 nM enzyme
Chlorobaculum tepidum
0.14
-
magnesium protoporphyrin
concentrations between 0.3 and 30 microM in the presence of 50 nM enzyme
Chlorobaculum tepidum
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Chlorobaculum tepidum
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli JM109, constitutive promoter on pUCmod, overexpression improved by using BL21 cells in combination with T7 promoter, subclconing into pET-20b(+) vector, engineered Escherichia coli strain overproducing protoporphyrin for activity assays
Chlorobaculum tepidum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0006
-
magnesium protoporphyrin
concentrations between 0.3 and 30 microM in the presence of 50 nM enzyme
Chlorobaculum tepidum
0.053
-
protoporphyrin
concentrations between 1 and 30 microM in the presence of 200 nM enzyme
Chlorobaculum tepidum
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant protein, gel filtration and SDS-PAGE
Chlorobaculum tepidum
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell culture
-
Chlorobaculum tepidum
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
activity assay in protoporphyrin overproducing Escherichia coli cells, interaction of subunits of the three magnesium chelatase complexes with magnesium protoporphyrin methyltransferase, differences in subunit interactions either increase or decrease methyltransferase activity, vice versa, activity of any of the three magnesium chelatase complexes not affected
Chlorobaculum tepidum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + magnesium protoporphyrin
different substrate specificity, protoporphyrin with or without bound metal as a substrate
687761
Chlorobaculum tepidum
S-adenosyl-L-homocysteine + magnesium protoporphyrin monomethyl ester
-
-
-
?
S-adenosyl-L-methionine + protoporphyrin
methyl transfer possible without bound metal, slow reaction rate
687761
Chlorobaculum tepidum
S-adenosyl-L-homocysteine + protoporphyrin monomethyl ester
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
majority of the protein exist as a high-molecular-weight multimer as determined by gel filtration
Chlorobaculum tepidum
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Chlorobaculum tepidum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0002
-
protoporphyrin
concentrations between 1 and 30 microM in the presence of 200 nM enzyme
Chlorobaculum tepidum
0.14
-
magnesium protoporphyrin
concentrations between 0.3 and 30 microM in the presence of 50 nM enzyme
Chlorobaculum tepidum
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Chlorobaculum tepidum
Other publictions for EC 2.1.1.11
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)
734272
Chen
Structural insights into the c ...
Synechocystis sp.
J. Biol. Chem.
289
25690-25698
2014
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734560
Tomiyama
Mg-chelatase I subunit 1 and M ...
Arabidopsis thaliana
J. Plant Res.
127
553-563
2014
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720712
Meinecke
Chlorophyll-deficient mutants ...
Chlamydomonas reinhardtii
Plant Mol. Biol.
72
643-658
2010
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695554
McLean
An enzyme-coupled continuous s ...
Synechocystis sp. PCC 6803
Anal. Biochem.
394
223-228
2009
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700486
Van Wilder
C1 metabolism and chlorophyll ...
Arabidopsis thaliana, Pisum sativum
New Phytol.
182
137-145
2009
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1
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2
2
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4
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687761
Johnson
Characterization of three homo ...
Chlorobaculum tepidum
J. Biol. Chem.
283
27776-27784
2008
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2
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1
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674841
Pontier
Knock-out of the magnesium pro ...
Arabidopsis thaliana
J. Biol. Chem.
282
2297-2304
2007
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1
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3
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1
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684982
Sawicki
S-adenosyl-L-methionine:magnes ...
Rhodobacter capsulatus
Biochem. J.
406
469-478
2007
1
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1
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5
4
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4
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660178
Alawady
Tobacco Mg protoporphyrin IX m ...
Nicotiana tabacum
Plant J.
41
282-290
2005
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660202
Alawady
Cloning and expression of the ...
Nicotiana tabacum
Plant Mol. Biol.
57
679-691
2005
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1
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661705
Shepherd
Kinetic basis for linking the ...
Synechocystis sp.
FEBS J.
272
4532-4539
2005
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657843
Shepherd
Transient kinetics of the reac ...
Synechocystis sp. PCC 6803
Biochem. J.
382
1009-1013
2004
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485113
Shepherd
Purification and kinetic chara ...
Synechocystis sp., Synechocystis sp. PCC 6803
Biochem. J.
371
351-360
2003
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485108
Block
The plant S-adenosyl-L-methion ...
Arabidopsis thaliana, Spinacia oleracea
Eur. J. Biochem.
269
240-248
2002
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485111
Averina
Native state, energetic intera ...
Hordeum vulgare
Indian J. Exp. Biol.
40
192-201
2002
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485112
Vothknecht
-
Sinefungin inhibits chlorophyl ...
Hordeum vulgare
Plant Physiol. Biochem.
33
759-763
1995
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485109
Gibson
The bacteriochlorophyll biosyn ...
Rhodobacter sphaeroides
FEBS Lett.
352
127-130
1994
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485110
Bollivar
Heterologous expression of the ...
Rhodobacter capsulatus
J. Bacteriol.
176
5290-5296
1994
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485102
Yee
Confirmation of a ping-pong me ...
Triticum aestivum
Biochem. Biophys. Res. Commun.
162
483-490
1989
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485104
Hinchigeri
-
The reaction mechanism of S-ad ...
Euglena gracilis
Photosynthetica
18
168-178
1984
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3
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485103
Hinchigeri
-
The purification and reaction ...
Rhodobacter sphaeroides
Photosynthetica
16
554-560
1982
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485106
Hinchigeri
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Purification of S-adenosyl-L-m ...
Hordeum vulgare
Photosynthetica
15
351-359
1981
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485107
Ellsworth
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Biosynthesis and inhibition of ...
Triticum aestivum
Photosynthetica
10
291-301
1976
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485105
Ellsworth
Activity and properties of (-) ...
Triticum aestivum
Biochim. Biophys. Acta
268
327-333
1972
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485101
Gibson
Studies on the biosynthesis of ...
Rhodobacter sphaeroides
Biochem. J.
88
325-334
1963
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