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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

Reaction

an N-acetyl-L-cysteine-S-conjugate
+
H2O
=
an L-cysteine-S-conjugate
 +
acetate

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 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.14 N-acyl-aliphatic-L-amino acid amidohydrolase

Engineering

Engineering on EC 3.5.1.14 - N-acyl-aliphatic-L-amino acid amidohydrolase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D274A
-
site-directed mutagenesis, the mutant shows 5695fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
H206A
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 560fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
H206K
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 348fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
H206N
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 11837fold reduced activity compared to the wild-type enzyme
I177A
I177L
L372A
2fold decreased KM-value compared to the wildtype with N-isopentanoyl-L-methionine
L372G
10fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
L372I
L372V
N263D
-
site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme
N263S
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 152fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
R276A
-
site-directed mutagenesis, dimerization domain mutant, the mutant shows 8995fold reduced activity compared to the wild-type enzyme, but the same expression and purification behaviour
R276N
-
site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme
R276Q
-
site-directed mutagenesis, dimerization domain mutant, nearly inactive mutant showing the same expression and purification behaviour compared to the wild-type enzyme
T347F
1.8fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
T347G
6.5fold increased KM-value compared to the wildtype with N-acetyl-L-methionine moiety
T347S
D68A
-
site-directed mutagenesis of AA3, the mutant is inactive
E167R
-
involved in substrate specificity
E177A
E177D
-
reduces the kcat value more than threefold
E24A
-
site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview
H116A
-
site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview
H21A
-
site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview
H21D
-
site-directed mutagenesis of AA3, metal content and activity compared to the wild-type enzyme, overview
N70A
-
site-directed mutagenesis of AA3, the mutant is active
R63A
-
site-directed mutagenesis of AA3, the mutant is inactive
R71A
-
site-directed mutagenesis of AA3, the mutant is active
Y287A
-
site-directed mutagenesis of AA3, the mutant is inactive
C102A
no hydrolytic activity
C102S
Km-values are similar to those of wild-type enzyme
E367Q
the kcat-value increases slightly, whereas the Km value does not change for N-acetyl-L-phenylalanine as substrates. Substrate inhibition of aminoacylase activity is also observed. The temperature-dependent activity and pH profile of the activity of E367Q are similar to those of wild-type enzyme
C102A
-
no hydrolytic activity
-
C102S
-
Km-values are similar to those of wild-type enzyme
-
E367Q
-
the kcat-value increases slightly, whereas the Km value does not change for N-acetyl-L-phenylalanine as substrates. Substrate inhibition of aminoacylase activity is also observed. The temperature-dependent activity and pH profile of the activity of E367Q are similar to those of wild-type enzyme
-
C23A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
C272A
site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme
C294A
site-directed mutagenesis, the mutation causes a conformational change of the 3D-structure, the mutant shows highly reduced activity compared to the wild-type enzyme
C331A
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
C49A
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
D82E
site-directed mutagenesis, the mutant shows highly reduced activity and loss of zinc coordination compared to the wild-type enzyme
D82N
site-directed mutagenesis, nearly inactive mutant
E147A
-
completely inactive
D346A
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis, by 4000fold, at pH 7.5, the pH optimum with substrate 3-(2-furyl)acryloyl-L-methionine is altered compared to the wild-type enzyme
D346E
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
D346N
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
D346Q
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5, the pH optimum with substrate 3-(2-furyl)acryloyl-L-methionine is altered compared to the wild-type enzyme
E146A
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
E146D
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
E146N
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
E146Q
site-directed mutagenesis, mutation of D346 significantly reduces the rates of both N-actyl-L-Met synthesis and hydrolysis at pH 7.5
D212Y
-
lower temperature stability than wild type protein
E336A
-
total knockout
E336I
-
total knockout
E336S
-
partial activity
F251K
-
impaired activity towards N-benzoyl-L-valine but not towards N-benzoyl-L-phenylalanine
F251R
-
impaired activity towards N-benzoyl-L-valine but not towards N-benzoyl-L-phenylalanine
F251Y
-
32% increase in activity towards N-benzoyl-L-valine, activity towards N-benzoyl-L-phenylalanine unaffected, tetrameric form retained after 1 h at 55°C like wild type protein
G246E/I274K
-
decreased activity on N-benzoyl-L-phenylalanine at higher temperature
H169N
-
lower activity than mutant protein H169R
H169Q
-
lower activity than mutant protein H169R
H169R
-
low activity
K226R/P234H/F251Y/I254N
-
37% increase in activity towards N-benzoyl-L-phenylalanine, lower temperature stability than wild type protein
L187F
-
may be involved in altering the relative flexibility or conformation
P237S
-
tetrameric form retained after 1 h at 55°C like wild type protein
S100T/M106K
-
51% increase in activity towards N-benzoyl-L-valine, activity towards N-benzoyl-L-phenylalanine unaffected
S100T/M106K/F251Y
-
no further improvement in activity (non-additive interaction between the mutated sites)
S217T/S244I/T250I
-
tetrameric form retained after 1 h at 55°C like wild type protein, decreased activity on N-benzoyl-L-phenylalanine at higher temperature
T299H
-
about 50% activity
T299K
-
about 50% activity
T306V
-
may be involved in altering the relative flexibility or conformation
V242D
-
32% increase in activity towards N-benzoyl-L-phenylalanine, lower temperature stability than wild type protein
additional information