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Literature summary extracted from

  • Wu, X.; Flatt, P.M.; Xu, H.; Mahmud, T.
    Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol from the endosymbiotic bacterium Actinomyces sp. Lu 9419 (2009), Chembiochem, 10, 304-314.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.3.33 overexpression in Escherichia coli BL21(DE3)pLysS Actinomyces sp.

Protein Variants

EC Number Protein Variants Comment Organism
5.1.3.33 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.
5.1.3.33 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.
5.1.3.33 E76G/E151G inactive mutant enzyme Actinomyces sp.
5.1.3.33 E76G/H99G inactive mutant enzyme Actinomyces sp.
5.1.3.33 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.
5.1.3.33 H14G/E151G inactive mutant enzyme Actinomyces sp.
5.1.3.33 H14G/E76G inactive mutant enzyme Actinomyces sp.
5.1.3.33 H14G/H99G inactive mutant enzyme Actinomyces sp.
5.1.3.33 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.
5.1.3.33 H99G/E151G inactive mutant enzyme Actinomyces sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.3.33 Co2+ can effectively rescue the activity of H99G mutant enzyme from which the metal ion has been removed with 1,10-phenanthroline Actinomyces sp.
5.1.3.33 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.
5.1.3.33 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.3.33 24000
-
 2 * 24000, polyhistidine-tagged protein, SDS-PAGE Actinomyces sp.
5.1.3.33 48000
-
 polyhistidine-tagged protein, gel filtration, nondenaturing-PAGE Actinomyces sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.3.33 2-epi-5-epi-valiolone Actinomyces sp. the enzyme is involved in the biosynthesis of cetoniacytone A 5-epi-valiolone
-
 ?
5.1.3.33 2-epi-5-epi-valiolone Actinomyces sp. Lu 9419 the enzyme is involved in the biosynthesis of cetoniacytone A 5-epi-valiolone
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.33 Actinomyces sp. A1YPR3
-
-
5.1.3.33 Actinomyces sp. Lu 9419 A1YPR3
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.1.3.33 2-epi-5-epi-valiolone = 5-epi-valiolone proposed reaction mechanism Actinomyces sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.33 2-epi-5-epi-valiolone the enzyme is involved in the biosynthesis of cetoniacytone A Actinomyces sp. 5-epi-valiolone
-
 ?
5.1.3.33 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 Actinomyces sp. 5-epi-valiolone
-
 ?
5.1.3.33 2-epi-5-epi-valiolone the enzyme is involved in the biosynthesis of cetoniacytone A Actinomyces sp. Lu 9419 5-epi-valiolone
-
 ?
5.1.3.33 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 Actinomyces sp. Lu 9419 5-epi-valiolone
-
 ?

Subunits

EC Number Subunits Comment Organism
5.1.3.33 homodimer 2 * 24000, polyhistidine-tagged protein, SDS-PAGE Actinomyces sp.

Synonyms

EC Number Synonyms Comment Organism
5.1.3.33 CetB
-
 Actinomyces sp.
5.1.3.33 EVE
-
 Actinomyces sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.3.33 30
-
 assay at Actinomyces sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.3.33 7.5
-
 assay at Actinomyces sp.

General Information

EC Number General Information Comment Organism
5.1.3.33 physiological function the enzyme is involved in the biosynthesis of cetoniacytone A Actinomyces sp.