2.1.1.169: tricetin 3',4',5'-O-trimethyltransferase
This is an abbreviated version!
For detailed information about tricetin 3',4',5'-O-trimethyltransferase, go to the full flat file.
Word Map on EC 2.1.1.169
Reaction
3 S-adenosyl-L-methionine
+
Synonyms
FOMT, O-methyltransferase, OMT2, TaCOMT1, TaOMT, TaOMT2
ECTree
2.1.1.169 tricetin 3',4',5'-O-trimethyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.1.1.169 - tricetin 3',4',5'-O-trimethyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D263E
D263I
D263N
E290I
E290Q
E322I
E322Q
G305A
G305S
H262F
H262L
H262R
N124I
N124Q
W259A
W259Y
D263E
severe loss of activity is due to a conflict between the catalytic His262-imidazole group and Glu-CH2
D263E
site-directed mutagenesis, severe loss of activity is due to a conflict between the catalytic His262-imidazole group and Glu-CH2
D263I
site-directed mutagenesis, Ile263 can not form a H-bond with 3'-OH group, the mutant shows almost complete loss in activity
D263N
site-directed mutagenesis, slight decrease in activity due to a decreased electronegativity of Asn-N compared to Asp-O, that affects charge transfer to tricetin-OH groups
D263N
slight decrease in activity due to a decreased electronegativity of Asn-N compared to Asp-O, that affects charge transfer to tricetin-OH groups
E290I
loss of activity is due to the fact that Ile can not form a H-bond with the 4'-OH of tricetin
E290I
site-directed mutagenesis, almost complete loss of activity is due to the fact that Ile can not form a H-bond with the 4'-OH of tricetin
E290Q
no activity. This mutation results in a more extensive H-bonding that hinders charge transfer and affects B-ring flexibility
E290Q
site-directed mutagenesis, the mutation results in a more extensive H-bonding that hinders charge transfer and affects B-ring flexibility and almost complete loss in activity
E322I
Km increased compared to wild-type, kcat/Km decreased compared to wild-type. Loss of charge or a change in the side chain affects H-bonding with the neighboring residues, especially His262
E322I
site-directed mutagenesis, loss of charge or a change in the side chain affects H-bonding with the neighboring residues, especially His262, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
E322Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
G305A
Loss of activity due to loss of H-bonding with the amide group of the neighboring Asn348
G305A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, the mutation results in loss of activity due to loss of H-bonding with the amide group of the neighboring Asn348
G305S
Km increased compared to wild-type, kcat/Km decreased compared to wild-type. Change in polarity is less effective than chain length on catalytic activity
G305S
site-directed mutagenesis, change in polarity is less effective than chain length on catalytic activity
H262F
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H262L
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H262R
results in almost complete loss of protein expression. All mutant proteins lack imidazole ring that is critical for proton flow among His262, Asp263 and the substrate
H262R
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, the mutation results in almost complete loss of protein expression, all mutant proteins lack imidazole ring that is critical for proton flow among His262, Asp263 and the substrate
N124I
no activity. Mutation results in a decreased substrate binding but not protein folding. Mutations disrupt H-bonding with 5-OH group of tricetin
N124I
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme, the mutation results in a decreased substrate binding but not protein folding. Both mutations disrupt H-bonding with 5-OH group of tricetin
N124Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N124Q
no activity. Mutation results in a decreased substrate binding but not protein folding. Mutations disrupt H-bonding with 5-OH group of tricetin
W259A
Km increased compared to wild-type, kcat/Km decreased compared to wild-type. Ala can maintain the H-bonding network between Trp259, Glu290 and His262, wheras Tyr cannot
W259A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, Ala can maintain the H-bonding network between Trp259, Glu290 and His262, wheras Tyr cannot
W259Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W259Y
Km increased compared to wild-type, kcat/Km decreased compared to wild-type
