BRENDA - Enzyme Database
show all sequences of 6.1.3.1

Active multienzyme assemblies for long-chain olefinic hydrocarbon biosynthesis

Christenson, J.K.; Jensen, M.R.; Goblirsch, B.R.; Mohamed, F.; Zhang, W.; Wilmot, C.M.; Wackett, L.P.; J. Bacteriol. 199, e00890 (2017)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expression in Escherichia coli
Xanthomonas campestris
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1900000
-
gel filtration, ordered assemblies of proteins OleBCD
Xanthomonas campestris
Organism
Organism
UniProt
Commentary
Textmining
Xanthomonas campestris
WP_011035474
-
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant coexpression of tagged OleABCD proteins in Escherichia coli and purification over His6 and FLAG columns results in OleA separating, while OleBCD purifies together, irrespective of which of the four Ole proteins is tagged. Hydrocarbon biosynthetic activity of copurified OleBCD assemblies can be reconstituted by adding separately purified OleA
Xanthomonas campestris
Subunits
Subunits
Commentary
Organism
?
x * 58500, calculated, protein OleC
Xanthomonas campestris
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Xanthomonas campestris
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1900000
-
gel filtration, ordered assemblies of proteins OleBCD
Xanthomonas campestris
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant coexpression of tagged OleABCD proteins in Escherichia coli and purification over His6 and FLAG columns results in OleA separating, while OleBCD purifies together, irrespective of which of the four Ole proteins is tagged. Hydrocarbon biosynthetic activity of copurified OleBCD assemblies can be reconstituted by adding separately purified OleA
Xanthomonas campestris
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 58500, calculated, protein OleC
Xanthomonas campestris
Other publictions for EC 6.1.3.1
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
Synonyms
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)
741939
Christenson
beta-Lactone synthetase found ...
Arenimonas malthae, Lysobacter dokdonensis, Micrococcus luteus, Micrococcus luteus ATCC4698, Stenotrophomonas maltophilia, Xanthomonas campestris
Biochemistry
56
348-351
2017
-
-
-
-
-
-
-
-
-
-
-
12
-
6
-
-
-
-
-
-
-
-
18
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
12
-
-
-
-
-
-
-
-
18
-
-
-
-
-
-
-
-
-
-
5
5
-
-
-
742797
Christenson
Active multienzyme assemblies ...
Xanthomonas campestris
J. Bacteriol.
199
e00890
2017
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
742283
Kancharla
Stenotrophomonas maltophilia ...
Stenotrophomonas maltophilia
ChemBioChem
17
1426-1429
2016
-
-
1
-
-
-
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
4
-
1
-
-
-
4
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
4
-
-
-
-
-
1
1
-
4
4
741673
Sukovich
Structure, function, and insi ...
Shewanella oneidensis, Shewanella oneidensis MR-1 / ATCC 700550
Appl. Environ. Microbiol.
76
3842-3849
2010
-
-
-
-
-
-
-
-
-
-
-
-
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2
-
-
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-
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1
1
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