Literature summary for 2.3.1.216 extracted from

Morita, H.; Kondo, S.; Oguro, S.; Noguchi, H.; Sugio, S.; Abe, I.; Kohno, T.
Structural insight into chain-length control and product specificity of pentaketide chromone synthase from Aloe arborescens (2007), Chem. Biol., 14, 359-369.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure analysis, molecular replacement	Aloe arborescens

Protein Variants

Protein Variants	Comment	Organism
M207G	site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-2-methyl-2,3-dihydro-4H-chromen-4-one and 2,7-dihydroxy-5-[(4-hydroxy-2-oxo-2H-pyran-6-yl)methyl]-5-methyl-2,3-dihydro-4H-chromen-4-one, i.e. SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction	Aloe arborescens
M207G/N218A	site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G	Aloe arborescens
M207G/N218D	site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G	Aloe arborescens
M207G/N218E	site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G	Aloe arborescens
M207G/N218K	site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G	Aloe arborescens
M207G/N218Q	site-directed mutagenesis, the mutant enzyme, in contrast to the wild-type, efficiently catalyzes the successive condensation of eight molecules of malonyl-CoA to produce SEK4 and SEK4b. The pentaketide-forming pentaketide chromone synthase is thus functionally transformed into an octaketide-producing enzyme by the single amino-acid substitution, the mutant performs a C-10/C-15 aldol-type cyclization reaction, the double mutant is almost functionally identical to the single mutant M207G	Aloe arborescens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5 malonyl-CoA	Aloe arborescens	-	5 CoA + 5,7-dihydroxy-2-methyl-4H-chromen-4-one + 5 CO2 + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Aloe arborescens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5 malonyl-CoA	-	Aloe arborescens	5 CoA + 5,7-dihydroxy-2-methyl-4H-chromen-4-one + 5 CO2 + H2O	-	?

Subunits

Subunits	Comment	Organism
homodimer	crystal structure analysis, molecular replacement, structure comparison, overview	Aloe arborescens

Synonyms

Synonyms	Comment	Organism
PCS	-	Aloe arborescens
pentaketide chromone synthase	-	Aloe arborescens

General Information

General Information	Comment	Organism
evolution	pentaketide chromone synthase is a plant-specific type III polyketide synthase that belongs to the chalcone synthase superfamily of type III polyketide synthases	Aloe arborescens
additional information	pentaketide chromone synthase residue Met207 is fairly flexible and adopts at least two distinct conformations, active site structure, catalytic residues of pentaketide chromone synthase are V351, M207, and L266, overview. Residues Cys143, Thr204, Met207, Leu266, and Val351 influence the catalytic activity and differentiate the enzyme from chalcone synthase, EC 2.3.1.74. The pentaketide chromone synthase crystal structure reveals neither a hydrogen-bond network, nor any additional catalytic Cys residues that appears to be crucial for the enzyme reaction	Aloe arborescens

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Release 2023.1 (January 2023)