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
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General Information
General Information on EC 3.5.1.81 - N-Acyl-D-amino-acid deacylase
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evolution
malfunction
additional information
the enzyme is a protein of 495 amino acids with a relatively low sequence similarity to a N-acyl-D-amino acid amidohydrolase from Alcaligenes faecalis DA1 (termed AFD), a binuclear zinc enzyme of the alpha/beta-barrel amidohydrolase superfamily. The unique cysteine residue that serves as a ligand to the active-site zinc ions in AFD and other N-acyl-D-amino acid amidohydrolases is not conserved in AcyM and is replaced by alanine. AcyM is the most closely related to a N-acyl-D-amino acid amidohydrolase of Gluconobacter oxydans (termed Gox1177) and phylogenetically distant from AFD and all other N-acyl-D-amino acid amidohydrolases that have been biochemically characterized. AcyM, along with Gox1177, appears to represent a new phylogenetic subcluster of N-acyl-D-amino acid amidohydrolases
evolution
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the enzyme is a protein of 495 amino acids with a relatively low sequence similarity to a N-acyl-D-amino acid amidohydrolase from Alcaligenes faecalis DA1 (termed AFD), a binuclear zinc enzyme of the alpha/beta-barrel amidohydrolase superfamily. The unique cysteine residue that serves as a ligand to the active-site zinc ions in AFD and other N-acyl-D-amino acid amidohydrolases is not conserved in AcyM and is replaced by alanine. AcyM is the most closely related to a N-acyl-D-amino acid amidohydrolase of Gluconobacter oxydans (termed Gox1177) and phylogenetically distant from AFD and all other N-acyl-D-amino acid amidohydrolases that have been biochemically characterized. AcyM, along with Gox1177, appears to represent a new phylogenetic subcluster of N-acyl-D-amino acid amidohydrolases
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replacement of methionine M221 with leucine in the enzyme successfully enhances the oxidative resistance, half-life, and enzyme activity
malfunction
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replacement of methionine M221 with leucine in the enzyme successfully enhances the oxidative resistance, half-life, and enzyme activity
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structure comparison of wild-type and mutant enzyme with the enzyme from Alcaligenes faecalis DA1, homology modeling, overview
additional information
amino acid residues Phe191, Leu298, Tyr344, and Met346 interact with the side chain of the substrate
additional information
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amino acid residues Phe191, Leu298, Tyr344, and Met346 interact with the side chain of the substrate
additional information
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amino acid residues Phe191, Leu298, Tyr344, and Met346 interact with the side chain of the substrate
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additional information
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structure comparison of wild-type and mutant enzyme with the enzyme from Alcaligenes faecalis DA1, homology modeling, overview
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