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2.3.1.65: bile acid-CoA:amino acid N-acyltransferase

This is an abbreviated version!
For detailed information about bile acid-CoA:amino acid N-acyltransferase, go to the full flat file.

Word Map on EC 2.3.1.65

Reaction

choloyl-CoA
+
glycine
=
CoA
+
glycocholate

Synonyms

acyltransferase, glycine-taurine N-, amino acid N-choloyltransferase, BAAT, BAATP1, BACAT, BAT, bile acid CoA: amino acid N-acyltransferase, bile acid CoA:amino acid N-acyltransferase, bile acid CoA:N-acyltransferase, bile acid coenzyme A-amino acid N-acyltransferase, bile acid coenzyme A: amino acid N-acyltransferase, bile acid coenzyme A:amino acid N-acyltransferase, bile acid-CoA:amino acid N acyltransferase, bile acid-CoA:amino acid N-acyltransferase, bile acid–coenzyme A:amino acid N-acyltransferase, glycine-taurine N-acyltransferase, hBAT, mBAT, rBAT

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.65 bile acid-CoA:amino acid N-acyltransferase

Engineering

Engineering on EC 2.3.1.65 - bile acid-CoA:amino acid N-acyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BAAT-12AA Trunc
-
mutant enzyme BAAT-12AA Trunc with 12 removed carboxy-terminal amino acids (407-418)
BAAT-Ex1Del
-
the amino (N)-terminal truncated mutant enzyme BAAT-Ex1Del possess no detectable N-acyltransferase activity
BAAT-S
-
the mutant BAAT-S, lacking the final two amino acids, shows slightly reduced enzyme activity
BAAT-SKL
-
mutant BAAT-SKL with a canonical PTS sequence has greater than a 2.5fold increase in N-acyltransferase activity compared with wild type enzyme using cholyl-CoA and taurine as substrates
C235A
-
activity is less than 0.4% of the wild-type activity
C235S
C372A
-
mutant with low enzyme activity
D326A
-
activity is less than 0.4% of the wild-type activity
D328A
-
inactive enzyme
H362A
-
inactive enzyme
H362Q
-
activity is less than 0.4% of the wild-type activity
additional information
-
the cytosolic enzyme localization is due to a carboxyterminal non-consensus peroxisomal targeting signal, SQL, since mutation of the SQL to SKL results in BAAT being efficiently imported into peroxisomes