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
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2.3.1.65
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peroxisomal
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unconjugated
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acyl-coas
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thioesterases
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cholyl-coa
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acid-conjugating
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hbats
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gallbladder
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proliferator
- 2.3.1.65
- peroxisomal
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unconjugated
- acyl-coas
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thioesterases
- cholyl-coa
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acid-conjugating
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hbats
- gallbladder
- proliferator
Reaction
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
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Engineering
Engineering on EC 2.3.1.65 - bile acid-CoA:amino acid N-acyltransferase
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BAAT-12AA Trunc
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mutant enzyme BAAT-12AA Trunc with 12 removed carboxy-terminal amino acids (407-418)
BAAT-Ex1Del
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the amino (N)-terminal truncated mutant enzyme BAAT-Ex1Del possess no detectable N-acyltransferase activity
BAAT-S
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the mutant BAAT-S, lacking the final two amino acids, shows slightly reduced enzyme activity
BAAT-SKL
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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
C235S
additional information
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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
C235S
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mutation converts the enzyme into an efficient bile acid-CoA thioesterase