3.5.1.81: N-Acyl-D-amino-acid deacylase
This is an abbreviated version!
For detailed information about N-Acyl-D-amino-acid deacylase, go to the full flat file.
Word Map on EC 3.5.1.81
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3.5.1.81
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alcaligenes
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subsp
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xylosoxydans
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faecalis
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synthesis
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amidohydrolases
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binuclear
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l-aminoacylase
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denitrificans
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d-hydantoinase
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n-acylated
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semi-synthetic
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dnak-dnaj-grpe
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d-leucine
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d-methionine
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industry
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biotechnology
- 3.5.1.81
- alcaligenes
-
subsp
- xylosoxydans
- faecalis
- synthesis
-
amidohydrolases
-
binuclear
- l-aminoacylase
- denitrificans
- d-hydantoinase
-
n-acylated
-
semi-synthetic
-
dnak-dnaj-grpe
- d-leucine
- d-methionine
- industry
- biotechnology
Reaction
Synonyms
AcyM, AxD-NAase, D-AAase, D-AGase, D-amidohydrolase, D-Amino acylase, D-Aminoacylase, D-ANase, D-NAase, DAA, dan, N-Acyl-D-amino acid amidohydrolase, N-acyl-D-amino-acid deacylase, N-Acyl-D-aspartate amidohydrolase, N-acyl-D-glutamate amidohydrolase, N-D-AAase
ECTree
3.5.1.81 N-Acyl-D-amino-acid deacylaseAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.5.1.81 - N-Acyl-D-amino-acid deacylase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl)-carbodiimide
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16% inhibition at 1 mM, 45% inhibition at 10 mM
2,4,6-Trinitrobenzene-1-sulfonate
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40% inhihition at 1 mM, 86% inhibition at 10 mM
4-(2-aminoethyl)benzenesulfonyl fluoride hydrochloride
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17% inhibition at 1 mM, 42% inhibition at 10 mM
diethyl dicarbonate
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93% inhibition by 93 mM, complete inhibition by 10 mM
N-acetyl-D-phenylalanine
substrate inhibition at high concentrations
N-Acetylimidazole
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88% inhibition at 1 mM, 96% inhibition at 10 mM
Cd2+
noncompetitive, binds at the alpha1 subsite ligated by His67, His69 and Asp366
Cu2+
noncompetitive, binds at the alpha2 subsite chelated by His67, His69 and Cys96
EDTA
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activity is fully restored by Co2+, and partially restored by Zn2+
Zn2+
noncompetitive, binds at the alpha1 subsite ligated by His67, His69 and Asp366
additional information
no inhibition by Ni2+, Co2+, Mg2+, Mn2+ and Ca2+
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additional information
no inhibition by 1 mM of by CaCl2, CoCl2, FeCl2, MnCl2, or CdCl2
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additional information
Met221 spatial closeness to the zinc-assistant catalytic center is highly potential as the primary site for oxidative inactivation of the enzyme via its methionine residue
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