BRENDA - Enzyme Database show
show all sequences of 5.1.3.33

Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol from the endosymbiotic bacterium Actinomyces sp. Lu 9419

Wu, X.; Flatt, P.M.; Xu, H.; Mahmud, T.; Chembiochem 10, 304-314 (2009)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpression in Escherichia coli BL21(DE3)pLysS
Actinomyces sp.
Engineering
Amino acid exchange
Commentary
Organism
E151G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
Actinomyces sp.
E76G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
Actinomyces sp.
E76G/E151G
inactive mutant enzyme
Actinomyces sp.
E76G/H99G
inactive mutant enzyme
Actinomyces sp.
H14G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
Actinomyces sp.
H14G/E151G
inactive mutant enzyme
Actinomyces sp.
H14G/E76G
inactive mutant enzyme
Actinomyces sp.
H14G/H99G
inactive mutant enzyme
Actinomyces sp.
H99G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
Actinomyces sp.
H99G/E151G
inactive mutant enzyme
Actinomyces sp.
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
can effectively rescue the activity of H99G mutant enzyme from which the metal ion has been removed with 1,10-phenanthroline
Actinomyces sp.
additional information
each monomer contains two beta,alpha,beta,beta,beta scaffolds that form a metal binding site with two histidine and two glutamic acid residues
Actinomyces sp.
Ni2+
can effectively rescue the activity of H99G mutant enzyme from which the metal ion has been removed with 1,10-phenanthroline
Actinomyces sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
24000
-
2 * 24000, polyhistidine-tagged protein, SDS-PAGE
Actinomyces sp.
48000
-
polyhistidine-tagged protein, gel filtration, nondenaturing-PAGE
Actinomyces sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-epi-5-epi-valiolone
Actinomyces sp.
the enzyme is involved in the biosynthesis of cetoniacytone A
5-epi-valiolone
-
-
?
2-epi-5-epi-valiolone
Actinomyces sp. Lu 9419
the enzyme is involved in the biosynthesis of cetoniacytone A
5-epi-valiolone
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Actinomyces sp.
A1YPR3
-
-
Actinomyces sp. Lu 9419
A1YPR3
-
-
Reaction
Reaction
Commentary
Organism
2-epi-5-epi-valiolone = 5-epi-valiolone
proposed reaction mechanism
Actinomyces sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-epi-5-epi-valiolone
the enzyme is involved in the biosynthesis of cetoniacytone A
729590
Actinomyces sp.
5-epi-valiolone
-
-
-
?
2-epi-5-epi-valiolone
no activity with 1L-epi-2-inosose, D-(+)-gluconic acid delta-lactone, D-mannose, shikimic acid, dehydroshikimic acid, and aminodehydroshikimic acid
729590
Actinomyces sp.
5-epi-valiolone
-
-
-
?
2-epi-5-epi-valiolone
the enzyme is involved in the biosynthesis of cetoniacytone A
729590
Actinomyces sp. Lu 9419
5-epi-valiolone
-
-
-
?
2-epi-5-epi-valiolone
no activity with 1L-epi-2-inosose, D-(+)-gluconic acid delta-lactone, D-mannose, shikimic acid, dehydroshikimic acid, and aminodehydroshikimic acid
729590
Actinomyces sp. Lu 9419
5-epi-valiolone
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 24000, polyhistidine-tagged protein, SDS-PAGE
Actinomyces sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Actinomyces sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Actinomyces sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression in Escherichia coli BL21(DE3)pLysS
Actinomyces sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E151G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
Actinomyces sp.
E76G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
Actinomyces sp.
E76G/E151G
inactive mutant enzyme
Actinomyces sp.
E76G/H99G
inactive mutant enzyme
Actinomyces sp.
H14G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
Actinomyces sp.
H14G/E151G
inactive mutant enzyme
Actinomyces sp.
H14G/E76G
inactive mutant enzyme
Actinomyces sp.
H14G/H99G
inactive mutant enzyme
Actinomyces sp.
H99G
in the absence of 1,10-phenanthroline, the activity of the single mutant variant is similar to that of the wild type
Actinomyces sp.
H99G/E151G
inactive mutant enzyme
Actinomyces sp.
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
can effectively rescue the activity of H99G mutant enzyme from which the metal ion has been removed with 1,10-phenanthroline
Actinomyces sp.
additional information
each monomer contains two beta,alpha,beta,beta,beta scaffolds that form a metal binding site with two histidine and two glutamic acid residues
Actinomyces sp.
Ni2+
can effectively rescue the activity of H99G mutant enzyme from which the metal ion has been removed with 1,10-phenanthroline
Actinomyces sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
24000
-
2 * 24000, polyhistidine-tagged protein, SDS-PAGE
Actinomyces sp.
48000
-
polyhistidine-tagged protein, gel filtration, nondenaturing-PAGE
Actinomyces sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-epi-5-epi-valiolone
Actinomyces sp.
the enzyme is involved in the biosynthesis of cetoniacytone A
5-epi-valiolone
-
-
?
2-epi-5-epi-valiolone
Actinomyces sp. Lu 9419
the enzyme is involved in the biosynthesis of cetoniacytone A
5-epi-valiolone
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-epi-5-epi-valiolone
the enzyme is involved in the biosynthesis of cetoniacytone A
729590
Actinomyces sp.
5-epi-valiolone
-
-
-
?
2-epi-5-epi-valiolone
no activity with 1L-epi-2-inosose, D-(+)-gluconic acid delta-lactone, D-mannose, shikimic acid, dehydroshikimic acid, and aminodehydroshikimic acid
729590
Actinomyces sp.
5-epi-valiolone
-
-
-
?
2-epi-5-epi-valiolone
the enzyme is involved in the biosynthesis of cetoniacytone A
729590
Actinomyces sp. Lu 9419
5-epi-valiolone
-
-
-
?
2-epi-5-epi-valiolone
no activity with 1L-epi-2-inosose, D-(+)-gluconic acid delta-lactone, D-mannose, shikimic acid, dehydroshikimic acid, and aminodehydroshikimic acid
729590
Actinomyces sp. Lu 9419
5-epi-valiolone
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 24000, polyhistidine-tagged protein, SDS-PAGE
Actinomyces sp.
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Actinomyces sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Actinomyces sp.
General Information
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of cetoniacytone A
Actinomyces sp.
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of cetoniacytone A
Actinomyces sp.
Other publictions for EC 5.1.3.33
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)
729590
Wu
Biosynthetic gene cluster of c ...
Actinomyces sp., Actinomyces sp. Lu 9419
Chembiochem
10
304-314
2009
-
-
1
-
10
-
-
-
-
3
2
2
-
6
-
-
-
1
-
-
-
-
4
1
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
10
-
-
-
-
-
-
3
2
2
-
-
-
-
-
-
-
-
4
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-