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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
N131D
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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
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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
N131L
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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
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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
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
A162T
same reactivity as wild type
A162T
-
2fold increase in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 2.9fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 1.8fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 2.8fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, no activity against protocatechuic acid
F172Y
no reaction with caffeic acid, with other substrates same reactivity as wild type
F172Y
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3fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 34fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 2.3fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, no activity with caffeic acid and protocatechuic acid
H183K
no reaction with caffeic acid, with other substrates same reactivity as wild type
H183K
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19fold decrease in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 1.8fold 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
L136Y
same reactivity as wild type
L136Y
-
1.5 fold increase in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 4.8fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 1.7fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 3.9fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, 176fold decrease in ratio of Vmax to Km-value for protocatechuic acid compared to wild-type enzyme
M130L
no reaction with caffeic acid and 5-hydroxyferulic acid, with other substrates same reactivity as wild type
M130L
-
3.1fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 51fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 5.8fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme,no activity with caffeic acid and protocatechuic acid
N131K
same reactivity as wild type
N131K
-
3.2 fold increase in ratio of Vmax to Km-value for caffeic acid compared to wild-type value, 2.9fold decrease in ratio of Vmax to Km-value for 5-hydroxy coniferaldehyde compared to wild-type enzyme, 1.7fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 2.8fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, 3.3fold decrease in ratio of Vmax to Km-value for protocatechuic acid compared to wild-type enzyme
N324Y
no reaction with caffeic acid, with other substrates same reactivity as wild type
N324Y
-
31.7fold 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, 10.2fold decrease in ratio of Vmax to Km-value for protocatechuic aldehyde compared to wild-type enzyme, 1.7fold decrease in ratio of Vmax to Km-value for 3,4-dihydroxy-5-methoxybenzaldehyde compared to wild-type enzyme, no activity with protocatechuic acid
additional information
the brown-midrib-3 mutant is disrupted in the caffeic acid O-methyltransferase gene with nearly null COMT activity
additional information
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the brown-midrib-3 mutant is disrupted in the caffeic acid O-methyltransferase gene with nearly null COMT activity