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2.1.1.6: catechol O-methyltransferase

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

Word Map on EC 2.1.1.6

Reaction

S-adenosyl-L-methionine
+
a catechol
=
S-adenosyl-L-homocysteine
 +
a guaiacol

Synonyms

catechol methyltransferase, catechol-O-methyl transferase, catechol-O-methyl transferase, membrane bound, catechol-O-methyl transferase, soluble, catechol-O-methyltransferase, catechol-O-transferase, catecholamine O-methyltransferase, COMT, COMT I, COMT II, COMT-mb, COMT-s, COMT1, COMT2, CTOMT1, L-COMT, MB-COMT, methyltransferase, catechol, S-COMT, SCOMT

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.6 catechol O-methyltransferase

Engineering

Engineering on EC 2.1.1.6 - catechol O-methyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C69S
-
mutation makes variant 108V and 108M more sensitive to oxidation
C95S
-
mutation increases the activity measured in absence of dithiothreitol in both the 108V and the 108M variant
L16P
-
missense mutation
V108M
V158M
the mutation affects directly COMT enzyme activity, the COMT polymorphism is unconnected to cold pain
Y71X
-
the mutation is predicted to truncate the protein before the catalytic domain likely affecting methyltransferase activity
K144A
mutation of the proposed catalytic Lys residue, does not abolish COMT activity
K144A/V173Y
shift towards para-selectivity
M91I/Y95C
active site humanized enzyme
W38D
mutation of hydrophobic pocket, approximately +93% regioisomeric excess, and around 50% conversion of substrate 3,4-dihydroxybenzaldehyde
W38K
mutant favors para- over meta-methylation of dihydroxy substrates
W38R
mutant favors para- over meta-methylation of dihydroxy substrates
Y200L
mutant favors meta- over para-methylation of dihydroxy substrates, and exhibits the greatest meta-selectivity whilst retaining relative activity similar to that of the wild-type
D162A
loss of S-adenosylmethionine binding
E106A
loss of S-adenosylmethionine binding
H163A
loss of S-adenosylmethionine binding
I56A
dissociation constant of S-adenosylmethionine is similar to wild-type. Residue I56 forms a pair of H-bonds with oxygen in the methionine portion
S86A
loss of S-adenosylmethionine binding
V107A
significant decrease in S-adenosylmethionine binding
W164A
dissociation constant of S-adenosylmethionine is similar to wild-type. Residue W164 forms a T-shaped pi-pi interaction with the adenine ring
D162A
-
loss of S-adenosylmethionine binding
-
E106A
-
loss of S-adenosylmethionine binding
-
H163A
-
loss of S-adenosylmethionine binding
-
S86A
-
loss of S-adenosylmethionine binding
-
W164A
-
dissociation constant of S-adenosylmethionine is similar to wild-type. Residue W164 forms a T-shaped pi-pi interaction with the adenine ring
-
additional information