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2.1.1.69: 5-hydroxyfuranocoumarin 5-O-methyltransferase

This is an abbreviated version!
For detailed information about 5-hydroxyfuranocoumarin 5-O-methyltransferase, go to the full flat file.

Word Map on EC 2.1.1.69

Reaction

S-adenosyl-L-methionine
+
a 5-hydroxyfurocoumarin
=
S-adenosyl-L-homocysteine
 +
a 5-methoxyfurocoumarin

Synonyms

bergaptol O-methyltransferase, bergaptol-5-O-methyltransferase, BMT, EC 2.1.1.92, furanocoumarin 5-methyltransferase, furanocoumarin 5-O-methyltransferase, methyltransferase, bergaptol

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.69 5-hydroxyfuranocoumarin 5-O-methyltransferase

Engineering

Engineering on EC 2.1.1.69 - 5-hydroxyfuranocoumarin 5-O-methyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D226A
the mutant is almost inactive
F171A
the mutant is almost inactive
G203A
the mutant shows about 75% of wild type activity
H264A
the mutant is almost inactive
I157F/V320I
the mutant shows about 4fold increased activity compared to the wild type enzyme
I157H
the mutant shows strongly reduced activity compared to the wild type enzyme
I157Y
the mutant shows about 2.4fold increased activity compared to the wild type enzyme
I157Y/S265F/V315N
the mutant shows severely reduced activity compared to the wild type enzyme
I157Y/S265N
the mutant shows about 1.5fold increased activity compared to the wild type enzyme
L122F
the mutant shows reduced activity compared to the wild type enzyme
L122H
the mutant shows severely reduced activity compared to the wild type enzyme
L122H/W261H
the mutant shows reduced severely activity compared to the wild type enzyme
L122H/W261H/H126F
the mutant shows severely reduced activity compared to the wild type enzyme
L122H/W261H/H126W
the mutant shows severely reduced activity compared to the wild type enzyme
L312A
the mutant is almost inactive
M175A
the mutant is almost inactive
M316A
the mutant shows about 70% of wild type activity
S265I
the mutant shows about 2.5fold increased activity compared to the wild type enzyme
S265N
the mutant shows about 1.9fold increased activity compared to the wild type enzyme
V315F
the mutant shows severely reduced activity compared to the wild type enzyme
V320I
high-catalytic activity mutant with about 8.5fold increased activity compared to the wild type enzyme
V320Y
the mutant shows reduced activity compared to the wild type enzyme
W261H
the mutant shows about 1.9fold increased activity compared to the wild type enzyme
W261L
the mutant shows slightly reduced activity compared to the wild type enzyme
Y319A
the mutant shows about 60% of wild type activity
Y319F
the mutant shows about 5fold increased activity compared to the wild type enzyme