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Literature summary for 5.1.3.33 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
Search for more literature for 5.1.3.33

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment 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 Comment 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] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
Actinomyces sp. A1YPR3
-
-
Actinomyces sp. Lu 9419 A1YPR3
-
-

Reaction

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
CetB
-
 Actinomyces sp.
EVE
-
 Actinomyces sp.

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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