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E26A
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22-32fold decrease in the kcat relative to that of the wild type, catalytic efficiency is less than 10% of wild-type. Residue E26 is the general base in catalysis
H206A
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3-4-old decrease in the kcat and an increase in the Km for both acetyl-CoA (7fold) and histamine (4fold)
P27A
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38-42fold decrease in the kcat
R138A
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2.4-2.8fold increase in kcat
S171A
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catalytic efficiency for acetyl-CoA and histamine are only 42 and 5.2% of that of the wild-type enzyme, respectively
T167A
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16-17fold decrease in kcat, catalytic efficiency is about 1% of wild-type
T167A/S171A
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catalytic efficiency for acetyl-CoA and histamine are only 5.1 and 0.28% of that of the wild-type enzyme, respectively
H120Q
crystallographic studies, role in enzymic reaction
H122Q
crystallographic studies, role in enzymic reaction
H122Q/H120Q
crystallographic studies, role in enzymic reaction
I57A/V59A
site-directed mutagenesis, the mutant shows reduced enzyme activity and altered inhibitor binding compared to the wild-type enzyme
P64A
site-directed mutagenesis, the mutant shows reduced enzyme activity and altered inhibitor binding compared to the wild-type enzyme
P64G
site-directed mutagenesis, the mutant shows reduced enzyme activity and altered inhibitor binding compared to the wild-type enzyme
P64W
site-directed mutagenesis, the mutant shows reduced enzyme activity and altered inhibitor binding compared to the wild-type enzyme
S205A
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1.6fold increase in Km-value for tryptamine compared to wild-type enzyme
T31A
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1.7fold increase in KM-value for tryptamine compared to wild-type enzyme
Y168F
crystallographic studies, role in enzymic reaction
C177A
fully active, not sensitive to oxidation or N-ethylmaleimide
C61A
fully active, not sensitive to oxidation or N-ethylmaleimide
H28Y
H28Y mutation in NAT is the cause of reduced NAT levels in vivo
S192V
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decrease in Km-value obtained by treatment with phorbol 12-myristate 13-acetate or forskolin is similar to the decrease observed in wild-type cells
T127V
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decrease in Km-value obtained by treatment with phorbol 12-myristate 13-acetate or forskolin is similar to the decrease observed in wild-type cells
T29V
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mutant enzyme shows an increase in Km-value obtained by treatment with phorbol 12-myristate 13-acetate or forskolin, decrease in Km-value is observed in wild-type cells
T29V/S203G
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mutant enzyme shows an increase in Km-value obtained by treatment with phorbol 12-myristate 13-acetate or forskolin, decrease in Km-value is observed in wild-type cells
additional information
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AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns
additional information
construction of the mutant strain and natural polymorphism, overview. The mutant Bm-iAANAT is expressed at higher levels in sclerified tissues, such as head, thoracic legs, and anal plate, than in less sclerified tissue, i.e. epidermis
additional information
construction of the mutant strain and natural polymorphism, overview. The mutant Bm-iAANAT is expressed at higher levels in sclerified tissues, such as head, thoracic legs, and anal plate, than in less sclerified tissue, i.e. epidermis
additional information
construction of the mutant strain and natural polymorphism, overview. The mutant Bm-iAANAT is expressed at higher levels in sclerified tissues, such as head, thoracic legs, and anal plate, than in less sclerified tissue, i.e. epidermis
additional information
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construction of the mutant strain and natural polymorphism, overview. The mutant Bm-iAANAT is expressed at higher levels in sclerified tissues, such as head, thoracic legs, and anal plate, than in less sclerified tissue, i.e. epidermis
additional information
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AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns
additional information
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AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns
additional information
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construction of truncation mutants AANAT 1-197(DELTAC8) and GST-AANAT 34-197 (DELTAN33, DELTAC8). Production of partially and differentially phosphorylated enzymes by semiprotein synthesis, overview
additional information
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single-nucleotide polymorphisms in AANAT found in Japanese population cannot be found in Caucasian population, genotyping, overview
additional information
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enhanced production of melatonin by ectopic overexpression of human serotonin N-acetyltransferase plays a role in cold resistance in transgenic rice seedlings. Leaves of transgenic lines S9 and S10 contain approximately 2.5fold and 1.9fold more chlorophyll, respectively, than those of the wild type
additional information
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AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns
additional information
phosphonodifluoromethylene alanine at Ser-205 is synthesized and fused to bacterially expressed AANAT30199 using expressed protein ligation. The resulting semisynthetic protein has enhanced affinity for the expressed 14-3-3 protein and exhibits greater cellular stability in microinjection experiments, as compared with the unmodified AANAT
additional information
construction of truncation mutants with reduced enzyme activity
additional information
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AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns
additional information
-
AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns
additional information
-
AANAT2 diversification is limited by stabilizing selection conferring to the enzyme well conserved secondary and tertiary structures. Only a few changes in amino acids appeared sufficient to induce different enzyme activity patterns