BRENDA - Enzyme Database
show all sequences of 1.21.98.3

Aerobic and anaerobic Mg-protoporphyrin monomethyl ester cyclases in purple bacteria: a strategy adopted to bypass the repressive oxygen control system

Ouchane, S.; Steunou, A.S.; Picaud, M.; Astier, C.; J. Biol. Chem. 279, 6385-6394 (2004)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Rubrivivax gelatinosus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
43000
-
-
Rubrivivax gelatinosus
63000
-
-
Rubrivivax gelatinosus
86000
-
SDS-PAGE of truncated protein of 384 residues
Rubrivivax gelatinosus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rubrivivax gelatinosus
Q7X2C7
-
-
Purification (Commentary)
Commentary
Organism
recombinant protein, preparation is yellow-brown in color. Only a small fraction can be solubilized with urea (6 M), and most of the iron-sulfur cluster is degraded upon solubilization of inclusion bodies
Rubrivivax gelatinosus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
-
738567
Rubrivivax gelatinosus
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 63000, calculated, 2 * 43000, SDS-PAGE of truncated protein of 384 residues
Rubrivivax gelatinosus
Cofactor
Cofactor
Commentary
Organism
Structure
[4Fe-4S]-center
BchE sequence displays the conserved CXXXCXXC sequence essential for 4Fe-4S cluster formation and an active 4Fe-4S cluster is present in the protein. Isolated protein is yellow-brown in colour with an absorption peak around 410 nm
Rubrivivax gelatinosus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Rubrivivax gelatinosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
[4Fe-4S]-center
BchE sequence displays the conserved CXXXCXXC sequence essential for 4Fe-4S cluster formation and an active 4Fe-4S cluster is present in the protein. Isolated protein is yellow-brown in colour with an absorption peak around 410 nm
Rubrivivax gelatinosus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
43000
-
-
Rubrivivax gelatinosus
63000
-
-
Rubrivivax gelatinosus
86000
-
SDS-PAGE of truncated protein of 384 residues
Rubrivivax gelatinosus
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant protein, preparation is yellow-brown in color. Only a small fraction can be solubilized with urea (6 M), and most of the iron-sulfur cluster is degraded upon solubilization of inclusion bodies
Rubrivivax gelatinosus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
-
738567
Rubrivivax gelatinosus
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 63000, calculated, 2 * 43000, SDS-PAGE of truncated protein of 384 residues
Rubrivivax gelatinosus
Expression
Organism
Commentary
Expression
Rubrivivax gelatinosus
expression of the BchE gene is oxygen-independent
additional information
General Information
General Information
Commentary
Organism
physiological function
a BchE mutant is photosynthesis-deficient, produces bacteriochlorophyll only under high oxygenation and accumulates Mg-protoporphyrin monomethyl ester under low oxygenation and anaerobiosis. A double knockout mutant lacking both Bche and aerobic magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase AcsF is devoid of photosystem and accumulates Mg-protoporphyrin monomethyl ester under both conditions indicating the involvement of the two enzymes at the same step of the biosynthesis pathway. AcsF acts strictly under high oxygenation conditions, whereas BchE is involved when the oxygen tension drops
Rubrivivax gelatinosus
General Information (protein specific)
General Information
Commentary
Organism
physiological function
a BchE mutant is photosynthesis-deficient, produces bacteriochlorophyll only under high oxygenation and accumulates Mg-protoporphyrin monomethyl ester under low oxygenation and anaerobiosis. A double knockout mutant lacking both Bche and aerobic magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase AcsF is devoid of photosystem and accumulates Mg-protoporphyrin monomethyl ester under both conditions indicating the involvement of the two enzymes at the same step of the biosynthesis pathway. AcsF acts strictly under high oxygenation conditions, whereas BchE is involved when the oxygen tension drops
Rubrivivax gelatinosus
Expression (protein specific)
Organism
Commentary
Expression
Rubrivivax gelatinosus
expression of the BchE gene is oxygen-independent
additional information
Other publictions for EC 1.21.98.3
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)
737606
Yamanashi
Identification of the chlE gen ...
Cyanothece sp. PCC 7425, Cyanothece sp. PCC 7822
Biochem. Biophys. Res. Commun.
463
1328-1333
2015
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-
-
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7
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2
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2
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2
2
-
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-
744228
Yamanashi
Identification of the chlE ge ...
Cyanothece sp. PCC 7425, Cyanothece sp. PCC 7822, Rhodobacter capsulatus, Rhodobacter capsulatus SB1003
Biochem. Biophys. Res. Commun.
463
1328-1333
2015
-
-
3
-
1
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4
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9
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4
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3
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3
3
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1
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4
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4
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-
-
-
-
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6
6
-
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-
726735
Boldareva-Nuianzina
Distribution and origin of oxy ...
Citromicrobium sp. CV44, Methylobacteriaceae bacterium RM11-8-1, Rhodobaca bogoriensis, Rhodobaca bogoriensis DSM 18756, Rhodobacterales bacterium chep-kr, Roseinatronobacter monicus, Roseinatronobacter sp. khil, Roseobacter sp., Roseobacter sp. B09, Roseobacter sp. Zun_kholvo
Appl. Environ. Microbiol.
79
2596-2604
2013
-
-
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10
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8
8
-
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-
689645
Gough
A new method for isolating phy ...
Rhodobacter capsulatus, Rhodobacter capsulatus ATCC BAA-309
Plant Physiol. Biochem.
45
932-936
2007
-
1
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6
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1
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738567
Ouchane
Aerobic and anaerobic Mg-proto ...
Rubrivivax gelatinosus
J. Biol. Chem.
279
6385-6394
2004
-
-
1
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-
-
-
-
-
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3
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1
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1
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1
1
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1
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1
1
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3
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1
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1
1
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-
-
-
-
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1
1
1
1
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739563
Gough
Anaerobic chlorophyll isocycli ...
Rhodobacter capsulatus, Rhodobacter capsulatus ATCC BAA-309
Proc. Natl. Acad. Sci. USA
97
6908-6913
2000
-
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4
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6
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1
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1
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6
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1
1
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738495
Yang
Rhodobacter capsulatus genes i ...
Rhodobacter capsulatus, Rhodobacter capsulatus ATCC BAA-309
J. Bacteriol.
172
5001-5010
1990
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4
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1
1
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