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2.1.1.68: caffeate O-methyltransferase

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

Word Map on EC 2.1.1.68

Reaction

S-adenosyl-L-methionine
+
3,4-dihydroxy-trans-cinnamate
=
S-adenosyl-L-homocysteine
 +
3-methoxy-4-hydroxy-trans-cinnamate

Synonyms

3,4-dihydroxybenzaldehyde-O-methyltransferase, AtCOMT1, AtOMT1, benzenoid/phenylpropanoid meta/para-O-methyltransferase, Bmr12, Bradi3g16530, brown midrib 12, caffeate 3-O-methyltransferase, caffeate methyltransferase, caffeate/5-hydroxyferulate 3/5-O-methyltransferase, caffeic acid 3-O-methyltransferase, caffeic acid O-methyl-transferase, caffeic acid O-methyltransferase, caffeic acid O-methyltransferase 1, caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase, caffeic O-methyl transferase, CCOMT, COMT, COMT-3D, COMT1, COMT2, COMT4, COMT6, DOMT, FGCOMT1, Lp OMT1, O-methyltransferase, O-methytransferase, OMT, OMT1, OMT3, OsCOMT1, RsOMT1, RsOMT3, S-adenosyl-L-methionine:caffeic acid-O-methyltransferase, Sb07g003860, Van OMT-2, Van OMT-3

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.68 caffeate O-methyltransferase

Engineering

Engineering on EC 2.1.1.68 - caffeate O-methyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C296F
the mutant shows slight activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296F/Q310L
the mutant shows about 4.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296F/Q310L/V314T
the mutant shows 9.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296H
the mutant shows about 3fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296H/Q310L
the mutant shows about 3.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296H/Q310L/V314T
the mutant shows about 6.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296Y
the mutant shows about 2fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296Y/Q310L/V314T
the mutant shows about 8fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
C296Y/V314T
the mutant shows about 5.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
Q310L
the mutant shows about 2fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
Q310L/V314T
the mutant shows about 5.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
V314N
the mutant shows slight activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
V314T
the mutant shows about 2.5fold activity improvement in O-methylation of N-acetylserotonin compared to the wild type enzyme
H268L
complete loss of catalytic acitivity
A162T
F172Y
H183K
L136Y
M130L
N131D
-
9.5fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 2.4fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, no activity with protocatechuic aldehyde, 3,4-dihydroxy-5-methoxybenzaldehyde and protocatechuic acid
N131E
-
475fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 1.7fold increase in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, no activity with protocatechuic aldehyde, 3,4-dihydroxy-5-methoxybenzaldehyde and protocatechuic acid
N131K
N131L
-
23.8fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 2.5fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 5.7fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 1.5fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, no activity with protocatechuic acid
N324H/M130L
-
2.4fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 4.2fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 2.8fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 3.1fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, 6.7fold decrease in ratio of Vmax to Km-value for protocatechuic acid compared to wild-type enzyme
N324Y
A71V
mutation significantly reduces Klason lignin content and alters lignin composition resulting in a significantly reduced S/G ratio relative to wild-type
G225D
mutation greatly reduces protein accumulation and mutation significantly reduces Klason lignin content and alters lignin composition resulting in a significantly reduced S/G ratio relative to wild-type
G325S
mutation impairs enzyme activity compared to wild type and mutation significantly reduces Klason lignin content and alters lignin composition resulting in a significantly reduced S/G ratio relative to wild-type
P150L
mutation impairs enzyme activity and mutation significantly reduces Klason lignin content and alters lignin composition resulting in a significantly reduced S/G ratio relative to wild-type
additional information