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2.3.1.87: aralkylamine N-acetyltransferase

This is an abbreviated version!
For detailed information about aralkylamine N-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.87

Reaction

acetyl-CoA
+
a 2-arylethylamine
=
CoA
+
an N-acetyl-2-arylethylamine

Synonyms

AA-NAT, AANAT, AANAT1, AANAT2, AANAT3, AANATL7, AATNATL2, acetyl-CoA:aralkylamine N-acetyltransferase, acetyltransferase, arylalkylamine N-, arylalkylamine N-acetyltransferase, arylalkylamine N-acetyltransferase 1, arylalkylamine N-acetyltransferase 1a, arylalkylamine N-acetyltransferase 1b, arylalkylamine N-acetyltransferase 2, arylalkylamine N-acetyltransferase like 7, arylalkylamine N-acetyltransferase-2, Bm-iAANAT, Eis, hAANAT, More, MSMEG_3513, N-acetyltransferase, NAT, oAANAT, PA4534, PaaNAT, Rv2416c, serotonin acetylase, serotonin acetyltransferase, serotonin N-acetyltransferase, serotonin-N-acetyltransferase, SNA, SNAT, SNAT1, SNAT2

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.87 aralkylamine N-acetyltransferase

Engineering

Engineering on EC 2.3.1.87 - aralkylamine N-acetyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E26A
-
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
-
3-4-old decrease in the kcat and an increase in the Km for both acetyl-CoA (7fold) and histamine (4fold)
P27A
-
38-42fold decrease in the kcat
R138A
-
2.4-2.8fold increase in kcat
S171A
-
catalytic efficiency for acetyl-CoA and histamine are only 42 and 5.2% of that of the wild-type enzyme, respectively
T167A
-
16-17fold decrease in kcat, catalytic efficiency is about 1% of wild-type
T167A/S171A
-
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
-
1.6fold increase in Km-value for tryptamine compared to wild-type enzyme
T31A
-
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
-
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
-
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
-
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
-
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