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Literature summary extracted from

  • Cacho, R.A.; Thuss, J.; Xu, W.; Sanichar, R.; Gao, Z.; Nguyen, A.; Vederas, J.C.; Tang, Y.
    Understanding programming of fungal iterative polyketide synthases: the biochemical basis for regioselectivity by the methyltransferase domain in the lovastatin megasynthase (2015), J. Am. Chem. Soc., 137, 15688-15691.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.161 0.17
-
 (4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus
2.3.1.161 2
-
 3-oxohexanoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus
2.3.1.161 5.2
-
 3-oxooctanoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.161 (4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-S-ACP + NADPH + H+ Aspergillus terreus reaction of ketoreductase subunit, natural substrate. ACP = acyl-carrier protein (4E,6E)-2-methyl-3-hydroxyocta-4,6-dienoyl-S-ACP + NADP+
-
 ?
2.3.1.161 (4E,6E)-3-oxoocta-4,6-dienoyl-S-ACP + S-adenosyl-L-methionine Aspergillus terreus reaction of methyltransferase subunit, natural substrate. ACP = acyl-carrier protein (4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-S-ACP + S-adenosyl-L-homocysteine
-
 ?
2.3.1.161 2-methyl-3-oxohexanoyl-N-acetylcysteamine + NADPH + H+ Aspergillus terreus reaction of ketoreductase subunit, natural substrate 3-hydroxy-2-methylhexanoyl-N-acetylcysteamine + NADP+
-
 ?
2.3.1.161 3-oxohexanoyl-N-acetylcysteamine + NADPH + H+ Aspergillus terreus reaction of ketoreductase subunit, natural substrate 3-hydroxyhexanoyl-N-acetylcysteamine + NADP+
-
 ?
2.3.1.161 additional information Aspergillus terreus the methyltransferase domain displays methylation activity toward different beta-ketoacyl groups, it is exceptionally selective toward its naturally programmed beta-keto-dienyltetraketide substrate with respect to both chain length and functionalization. The ketoreductase domain displays broader substrate specificity toward different beta-ketoacyl groups ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.161 Aspergillus terreus Q9Y8A5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.161 (4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-S-ACP + NADPH + H+ reaction of ketoreductase subunit, natural substrate. ACP = acyl-carrier protein Aspergillus terreus (4E,6E)-2-methyl-3-hydroxyocta-4,6-dienoyl-S-ACP + NADP+
-
 ?
2.3.1.161 (4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine + S-adenosyl-L-methionine reaction of methyltransferase subunit, natural substrate analogue. ACP = acyl-carrier protein Aspergillus terreus (4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-N-acetylcysteamine + S-adenosyl-L-homocysteine
-
 ?
2.3.1.161 (4E,6E)-3-oxoocta-4,6-dienoyl-S-ACP + S-adenosyl-L-methionine reaction of methyltransferase subunit, natural substrate. ACP = acyl-carrier protein Aspergillus terreus (4E,6E)-2-methyl-3-oxoocta-4,6-dienoyl-S-ACP + S-adenosyl-L-homocysteine
-
 ?
2.3.1.161 2-methyl-3-oxohexanoyl-N-acetylcysteamine + NADPH + H+ reaction of ketoreductase subunit, natural substrate Aspergillus terreus 3-hydroxy-2-methylhexanoyl-N-acetylcysteamine + NADP+
-
 ?
2.3.1.161 3-oxohexanoyl-N-acetylcysteamine + NADPH + H+ reaction of ketoreductase subunit, natural substrate Aspergillus terreus 3-hydroxyhexanoyl-N-acetylcysteamine + NADP+
-
 ?
2.3.1.161 3-oxooctanoyl-N-acetylcysteamine + S-adenosyl-L-methionine reaction of methyltransferase subunit, artificial substrate. 0.3% of the activity with (4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine Aspergillus terreus 2-methyl-3-oxooctanoyl-N-acetylcysteamine + S-adenosyl-L-homocysteine
-
 ?
2.3.1.161 additional information the methyltransferase domain displays methylation activity toward different beta-ketoacyl groups, it is exceptionally selective toward its naturally programmed beta-keto-dienyltetraketide substrate with respect to both chain length and functionalization. The ketoreductase domain displays broader substrate specificity toward different beta-ketoacyl groups Aspergillus terreus ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.161 0.085
-
 2-methyl-3-oxohexanoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus
2.3.1.161 0.32
-
 3-oxooctanoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus
2.3.1.161 0.57
-
 3-oxohexanoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus
2.3.1.161 3.25
-
 (4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.161 additional information enzyme utilizes an oxidized quinone as cofactor Aspergillus terreus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.3.1.161 0.06
-
 3-oxooctanoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus
2.3.1.161 0.31
-
 3-oxohexanoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus
2.3.1.161 18.93
-
 (4E,6E)-3-oxoocta-4,6-dienoyl-N-acetylcysteamine pH not specified in the publication, temperature not specified in the publication Aspergillus terreus