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Literature summary for 2.3.1.212 extracted from

  • Shimokawa, Y.; Morita, H.; Abe, I.
    Benzalacetone synthase (2012), Front. Plant Sci., 3, 57.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.212

Application

Application Comment Organism
synthesis possibility of peparation of tetramic acids from various amino acids through the enzyme Rheum palmatum

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rheum palmatum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information steady-state enzyme kinetics Rheum palmatum
0.0033
-
 D-phenylalanyl-CoA pH 8.0, temperature not specified in the publication Rheum palmatum
0.0117
-
 L-phenylalanyl-CoA pH 8.0, temperature not specified in the publication Rheum palmatum
0.0237
-
 N-methylanthraniloyl-CoA pH 8.0, temperature not specified in the publication Rheum palmatum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-coumaroyl-CoA + malonyl-CoA + H2O Rheum palmatum
-
 2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Rheum palmatum Q94FV7
-
-

Reaction

Reaction Comment Organism Reaction ID
4-coumaroyl-CoA + malonyl-CoA + H2O = 2 CoA + 4-hydroxybenzalacetone + 2 CO2 the enzyme shows remarkable substrate tolerance and catalytic versatility, structure-function relationship and functional diversity of type III PKS enzymes, the enzyme catalytic mechanism for the thioester bond cleavage of the enzyme-bound diketide intermediate and the decarboxylation reaction to produce benzalacetone involves Cys164, His33, and Asn336, overview. RpBAS initially accepts the aminoacyl-CoA as a starter, and then recruits malonyl-CoA for a Claisen condensation to generate the gamma-amino-beta-ketothioester. The free gamma-amino group of the enzyme-bound intermediate can cleave the thioester bond, with concomitant intramolecular lactamization Rheum palmatum
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3 (2RS)-methylmalonyl-CoA + H2O
-
 Rheum palmatum 6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone + ? a methylated C9 triketide ?
4-coumaroyl-CoA + (2RS)-methylmalonyl-CoA + H2O
-
 Rheum palmatum 2 CoA + 1-(4-hydroxyphenyl)pent-1-en-3-one + 2 CO2 an unnatural novel diketide ?
4-coumaroyl-CoA + malonyl-CoA + H2O
-
 Rheum palmatum 2 CoA + 4-hydroxybenzalacetone + 2 CO2
-
 ?
D-phenylalanyl-CoA + malonyl-CoA
-
 Rheum palmatum ?
-
 ?
D-tryptophanyl-CoA + malonyl-CoA
-
 Rheum palmatum ?
-
 ?
L-phenylalanyl-CoA + malonyl-CoA
-
 Rheum palmatum ? the enzyme produces a 1:10 mixture of two products from L-phenylalanyl-CoA and malonyl-CoA. The minor product is a tetramic acid monomer, the major product is a tetramic acid dimer ?
L-tryptophanyl-CoA + malonyl-CoA
-
 Rheum palmatum ?
-
 ?
additional information RpBAS also accepts a series of aminoacyl-CoA thioesters as starter substrates, and catalyzes their condensation with one molecule of malonyl-CoA to produce the tetramic acid (2,4-pyrrolidinedione)derivatives. RpBAS also accepts (2RS)-methylmalonyl-CoA as the only substrate to produce a methylated C9 triketide, 6-ethyl-4-hydroxy-3,5-dimethyl-2-pyrone, as a single product from three molecules of (2RS)-methylmalonyl-CoA. Substrate specificity, overview Rheum palmatum ?
-
 ?
N-methylanthraniloyl-CoA + (2RS)-methylmalonyl-CoA
-
 Rheum palmatum 4-hydroxy-1,3-dimethyl-2(1H)-quinolone + ?
-
 ?

Synonyms

Synonyms Comment Organism
bAS
-
 Rheum palmatum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0247
-
 N-methylanthraniloyl-CoA pH 8.0, temperature not specified in the publication Rheum palmatum
0.135
-
 D-phenylalanyl-CoA pH 8.0, temperature not specified in the publication Rheum palmatum
0.463
-
 L-phenylalanyl-CoA pH 8.0, temperature not specified in the publication Rheum palmatum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.5
-
 Rheum palmatum

General Information

General Information Comment Organism
evolution the enzyme is a plant-specific type III polyketide synthase of the chalcone synthase (CHS) superfamily Rheum palmatum
physiological function pBAS catalyzes the one-step, decarboxylative condensation of 4-coumaroyl-CoA with malonyl-CoA to produce the C6-C4 benzalacetone scaffold Rheum palmatum