3.5.1.14: N-acyl-aliphatic-L-amino acid amidohydrolase
This is an abbreviated version!
For detailed information about N-acyl-aliphatic-L-amino acid amidohydrolase, go to the full flat file.
Word Map on EC 3.5.1.14
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3.5.1.14
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n-acetylated
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synthesis
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n-acetyl-l-methionine
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mercapturic
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acylases
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cobalt-activated
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medicine
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diagnostics
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analysis
- 3.5.1.14
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n-acetylated
- synthesis
- n-acetyl-l-methionine
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mercapturic
- acylases
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cobalt-activated
- medicine
- diagnostics
- analysis
Reaction
Synonyms
AA1, AA3, AAIII, ACY 1a, ACY 1b, ACY-1, ACY-1A, Acy1, acylase, acylase 1, acylase B, acylase I, alpha-N-acylaminoacid hydrolase, amido acid deacylase, aminoacylase, aminoacylase 1, aminoacylase 1a, aminoacylase 3, aminoacylase I, aminoacylase-1, aminoacylase-1A, aminoacylase-1B, benzamidase, D-AAse, D-Aminoacylase, dehydropeptidase II, DR_ACY, fatty acid-amino acid conjugate hydrolyzing aminoacylase 1, fMDF, fungus aminoacylase-1, hAcy1, hippurase, hippuricase, histozyme, HKA, hog intestinal acylase I, hog kidney aminoacylase, hog kidney aminoacylase I, intestine acylase I, L-ACY-1, L-amido-acid acylase, L-aminoacylase, LAA, lepidopteran aminoacylase 1, long acyl amidoacylase, M20, More, N-Acyl-D-aspartate amidohydrolase, N-acyl-L-amino acid amidohydrolase, N-acyl-L-amino acid hydrolase, N-acyl-L-amino-acid amidohydrolase, N-acyl-L-aminoacylase 1, N-acylase IA, N-formylmethionine deformylase, Nalpha-acyl-L-amino acid amidohydrolase, pAcy1, PhoACY, pig kidney aminoacylase, porcine kidney aminoacylase, short acyl amidoacylase, sphingosine kinase 1-interacting protein
ECTree
3.5.1.14 N-acyl-aliphatic-L-amino acid amidohydrolaseAdvanced search results
results (
results (Specific Activity
Specific Activity on EC 3.5.1.14 - N-acyl-aliphatic-L-amino acid amidohydrolase
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SPECIFIC ACTIVITY [µmol/min/mg] 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
0.00000028
substrate N-linolenoyl-L-glutamine, protein partially purified from frass, pH 8.0, 20°C
0.0006
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S100T/M106K mutant protein, substrate N-acetylpipecolic acid, pH 8.0, 55°C
0.003
0.005
-
F251K mutant protein, substrate N-benzoyl-L-isoleucine, pH 8.0, 55°C
0.008
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F251K mutant protein, substrate N-benzoyl-L-tert-leucine, pH 8.0, 55°C
0.0092
-
pH 8.0, temperature not specified in the publication, substrate: acetyl-DL-Trp
0.024
-
wild type protein, substrate N-acetylpipecolic acid, pH 8.0, 55°C
0.026
-
S100T/M106K mutant protein, substrate N-benzoyl-L-isoleucine, pH 8.0, 55°C
0.075
-
wild type protein, substrate N-benzoyl-L-tert-leucine, pH 8.0, 55°C
0.112
-
F251K mutant protein, substrate N-benzoyl-L-valine, pH 8.0, 55°C
0.19
-
wild type protein, substrate N-benzoyl-L-isoleucine, pH 8.0, 55°C
0.55
0.89
1.256
-
F251K mutant protein, substrate N-acetyl-L-phenylalanine, pH 8.0, 55°C
1.405
-
S100T/M106K mutant protein, substrate N-acetyl-L-phenylalanine, pH 8.0, 55°C
1.55
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S100T/M106K mutant protein, substrate N-benzoyl-L-phenylalanine, pH 8.0, 55°C
105
using 3 mM N-palmitoyl-L-Met as substrate, at 37°C, pH not specified in the publication
106
using 3 mM N-myristoyl-L-Met as substrate, at 37°C, pH not specified in the publication
14
169
using 3 mM N-butyryl-L-Met as substrate, at 37°C, pH not specified in the publication
17
using N-lauroyl-L-Cys as substrate, at 37°C, pH not specified in the publication
173
using 3 mM N-acetyl-L-Met as substrate, at 37°C, pH not specified in the publication
175
using 3 mM N-hexanoyl-L-Met as substrate, at 37°C, pH not specified in the publication
19
using N-acetyl-L-Phe as substrate, at 37°C, pH not specified in the publication
194
2.15
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F251K mutant protein, substrate N-benzoyl-L-phenylalanine, pH 8.0, 55°C
2.9
recombinant wild-type enzyme, substrate L-methionine, synthesis reaction, pH 6.0, 25°C
24
using N-acetyl-L-Val as substrate, at 37°C, pH not specified in the publication
251
using 3 mM N-octanoyl-L-Met as substrate, at 37°C, pH not specified in the publication
3.32
-
S100T/M106K mutant protein, substrate N-benzoyl-L-valine, pH 8.0, 55°C
31
using N-acetyl-L-Asn as substrate, at 37°C, pH not specified in the publication
34
using N-lauroyl-Gly as substrate, at 37°C, pH not specified in the publication
36
using N-lauroyl-L-Ser as substrate, at 37°C, pH not specified in the publication
4
using N-lauroyl-L-Arg as substrate, at 37°C, pH not specified in the publication
412
440
purified native wild-type enzyme, substrate N-acetyl-L-methionine, pH 7.5, 37°C
5.555
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wild type protein, substrate N-acetyl-L-phenylalanine, pH 8.0, 55°C
5.73
530
59
using N-acetyl-L-His as substrate, at 37°C, pH not specified in the publication
6.8
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wild type protein, substrate N-benzoyl-L-phenylalanine, pH 8.0, 55°C
60
using N-acetyl-L-Leu as substrate, at 37°C, pH not specified in the publication
66
using N-acetyl-L-Arg as substrate, at 37°C, pH not specified in the publication
72
using 3 mM N-lauroyl-L-Met as substrate, at 37°C, pH not specified in the publication
77
recombinant wild-type enzyme, substrate N-acetyl-L-methionine, hydrolytic reaction, pH 6.0, 25°C
89
using 3 mM N-decanoyl-L-Met as substrate, at 37°C, pH not specified in the publication
9.4
90
96
additional information
0.003
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F251K mutant protein, substrate N-acetylpipecolic acid, pH 8.0, 55°C
0.003
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S100T/M106K mutant protein, substrate N-benzoyl-L-tert-leucine, pH 8.0, 55°C
0.89
native wild-type enzyme, culture supernatant, substrate N-acetyl-L-methionine, pH 7.5, 37°C
0.89
recombinant wild-type enzyme, culture supernatant, substrate N-acetyl-L-methionine, pH 7.5, 37°C
14
using N-acetyl-L-Gln as substrate, at 37°C, pH not specified in the publication
14
using N-lauroyl-L-Lys as substrate, at 37°C, pH not specified in the publication
194
using N-acetyl-L-Ala as substrate, at 37°C, pH not specified in the publication
412
purified recombinant wild-type enzyme, substrate N-acetyl-L-cysteine, pH 7.5, 37°C
412
using N-acetyl-L-Cys as substrate, at 37°C, pH not specified in the publication
530
purified recombinant wild-type enzyme, substrate N-acetyl-L-methionine, pH 7.5, 37°C
530
using 15 mM N-acetyl-L-Met as substrate, at 37°C, pH not specified in the publication
6
using N-lauroyl-L-Asn as substrate, at 37°C, pH not specified in the publication
6
using N-lauroyl-L-His as substrate, at 37°C, pH not specified in the publication
8
using N-acetyl-Gly as substrate, at 37°C, pH not specified in the publication
8
using N-acetyl-L-Asp as substrate, at 37°C, pH not specified in the publication
96
purified recombinant wild-type enzyme, substrate N-lauryl-L-alanine, pH 7.5, 37°C
96
using N-lauroyl-L-Ala as substrate, at 37°C, pH not specified in the publication
additional information
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1.74 U/mg in phosphate buffer and 0.88 U/mg in 0.1M Tris-HCl buffer
additional information
substrate specificities of recombinant and native enzyme, overview
additional information
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substrate specificities of recombinant and native enzyme, overview
additional information
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maximum specific activity 22.25-27.75 U/ml at 40ºC and pH 7
