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Literature summary extracted from

  • McGuire, S.M.; Silva, J.C.; Casillas, E.G.; Townsend, C.A.
    Purification and characterization of versicolorin B synthase from Aspergillus parasiticus. Catalysis of the stereodifferentiating cyclization in aflatoxin biosynthesis essential to DNA interaction (1996), Biochemistry, 35, 11470-11486.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.143 3-(2-hydroxyethyl)-2,3-dihydro-1-benzofuran-2,4-diol competitive Aspergillus parasiticus
4.2.1.143 versicolorin B
-
 Aspergillus parasiticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.143 0.0024
-
 versiconal hemiacetal pH 6.5, 37°C Aspergillus parasiticus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.143 78000
-
 2 * 78000, SDS-PAGE Aspergillus parasiticus
4.2.1.143 140000
-
 gel filtration Aspergillus parasiticus

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.143 Aspergillus parasiticus Q12062
-
-
4.2.1.143 Aspergillus parasiticus ATCC 56775 Q12062
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.143
-
 Aspergillus parasiticus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.143 1900
-
 pH 6.5, 37°C Aspergillus parasiticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.143 additional information enzyme selects from two equilibrating enantiomers of versiconal hemiacetal to cyclize the appropriate antipode to optically pure versicolorin B. By varying the amount of enzyme to a fixed concentration of substrate, the rate of enzymic cyclization can be limited by the intrinsic rate of enantiomerization of the substrate under the conditions of reaction Aspergillus parasiticus ?
-
 ?
4.2.1.143 additional information enzyme selects from two equilibrating enantiomers of versiconal hemiacetal to cyclize the appropriate antipode to optically pure versicolorin B. By varying the amount of enzyme to a fixed concentration of substrate, the rate of enzymic cyclization can be limited by the intrinsic rate of enantiomerization of the substrate under the conditions of reaction Aspergillus parasiticus ATCC 56775 ?
-
 ?
4.2.1.143 versiconal hemiacetal i.e. (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione Aspergillus parasiticus versicolorin B + H2O (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione, ?
4.2.1.143 versiconal hemiacetal i.e. (2S,3S)-2,4,6,8-tetrahydroxy-3-(2-hydroxyethyl)anthra[2,3-b]furan-5,10-dione Aspergillus parasiticus ATCC 56775 versicolorin B + H2O (3aR,12bS)-8,10,12-trihydroxy-1,2,3a,12b-tetrahydroanthra[2,3-b]furo[3,2-d]furan-6,11-dione, ?

Subunits

EC Number Subunits Comment Organism
4.2.1.143 dimer 2 * 78000, SDS-PAGE Aspergillus parasiticus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.143 2.5
-
 versiconal hemiacetal pH 6.5, 37°C Aspergillus parasiticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.143 4 8 broad Aspergillus parasiticus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.1.143 4
-
 drastic decline in activity below Aspergillus parasiticus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.2.1.143 0.076
-
 3-(2-hydroxyethyl)-2,3-dihydro-1-benzofuran-2,4-diol pH 6.5, 37°C Aspergillus parasiticus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
4.2.1.143 Aspergillus parasiticus isoelectric focusing
-
 4.7