2.3.1.216: 5,7-dihydroxy-2-methylchromone synthase
This is an abbreviated version!
For detailed information about 5,7-dihydroxy-2-methylchromone synthase, go to the full flat file.
Word Map on EC 2.3.1.216
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2.3.1.216
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polyketide
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arborescens
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aloe
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condensations
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octaketide
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synthases
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nonaketide
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plant-specific
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unnatural
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naphthopyrone
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inert
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chalcone
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medicago
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hexaketide
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sativa
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longest
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iterative
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lining
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molecular biology
- 2.3.1.216
- polyketide
- arborescens
-
aloe
-
condensations
-
octaketide
- synthases
-
nonaketide
-
plant-specific
-
unnatural
-
naphthopyrone
-
inert
- chalcone
-
medicago
-
hexaketide
- sativa
-
longest
-
iterative
-
lining
- molecular biology
Reaction
5 malonyl-CoA
=
5 CoA
+
Synonyms
PCS, pentaketide chromone synthase
ECTree
2.3.1.216 5,7-dihydroxy-2-methylchromone synthaseAdvanced search results
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results (General Information
General Information on EC 2.3.1.216 - 5,7-dihydroxy-2-methylchromone synthase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
physiological function
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the plant-specific type III polyketide synthase that produces 5,7-dihydroxy-2-methylchromone from five molecules of malonyl-CoA. The aromatic pentaketide is a biosynthetic precursor of the anti-asthmatic furochromones kehellin and visnagin
additional information
evolution
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pentaketide chromone synthase is a plant-specific type III polyketide synthase that belongs to the chalcone synthase superfamily of type III polyketide synthases
evolution
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pentaketide chromone synthase is a plant-specific type III polyketide synthase that belongs to the chalcone synthase superfamily of type III polyketide synthases and grouped with other non-chalcone forming enzymes
additional information
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active site structure of wild-type and mutant enzymes, overview. Amino acid residue at position 197 in the active site governs the chain length of the polyketide. Leucine at position 256 in the active site for both oktaketide synthase and pentaketide chromone synthase influences the substrate preference for malonyl-CoA as a starting unit, while a glycine residue located in the same position and found in the catalytic pocket of chalcone synthase can possibly compel the enzyme to readily accept 4-coumaroyl-CoA as a starting unit
additional information
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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
additional information
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the critical active-site residue 197, and the catalytic triad, Cys164, His303, and Asn336, are conserved in type III polyketide synthases, while the residues lining the active-site are exchanged to M197, L256, V338 (numbering in Madia sativa CHS). Active-site architecture of pentaketide chromone synthase compared to other type III polyketide synthases, crystal structure and hmology modeling, overview
