EC Number | Cloned (Comment) | Organism |
---|---|---|
3.5.1.81 | DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis | Microbacterium natoriense |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.81 | CuCl2 | 93% inhibition at 1 mM | Microbacterium natoriense | |
3.5.1.81 | EDTA | 35% inhibition at 20 mM, low inhibition level | Microbacterium natoriense | |
3.5.1.81 | HgCl2 | 99% inhibition at 1 mM | Microbacterium natoriense | |
3.5.1.81 | additional information | no inhibition by 1 mM of by CaCl2, CoCl2, FeCl2, MnCl2, or CdCl2 | Microbacterium natoriense | |
3.5.1.81 | N-acetyl-D-phenylalanine | substrate inhibition at high concentrations | Microbacterium natoriense | |
3.5.1.81 | ZnCl2 | 96% inhibition at 1 mM | Microbacterium natoriense |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.81 | additional information | - |
additional information | Michaelis-Menten kinetics | Microbacterium natoriense | |
3.5.1.81 | 2.5 | - |
N-acetyl-D-phenylalanine | pH 7.0, 37°C | Microbacterium natoriense |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.5.1.81 | additional information | 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 | Microbacterium natoriense |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.5.1.81 | 56000 | - |
1 * 56000, SDS-PAGE | Microbacterium natoriense |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.81 | N-acetyl-D-phenylalanine + H2O | Microbacterium natoriense | - |
acetate + D-phenylalanine | - |
? | |
3.5.1.81 | N-acetyl-D-phenylalanine + H2O | Microbacterium natoriense TNJL143-2 | - |
acetate + D-phenylalanine | - |
? | |
3.5.1.81 | N-acyl-D-amino acid + H2O | Microbacterium natoriense | - |
a carboxylate + D-amino acid | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.81 | Microbacterium natoriense | I7HFV7 | - |
- |
3.5.1.81 | Microbacterium natoriense TNJL143-2 | I7HFV7 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.5.1.81 | native enzyme 77fold to homogeneity by dialysis, several steps of anion exchange chromatography and one step of hydrophobic interaction chromatography, followed by gel filtration | Microbacterium natoriense |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.5.1.81 | culture condition:N-acetyl-DL-phenylalanine-grown cell | - |
Microbacterium natoriense | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.81 | additional information | no activity with N-acetyl-L-amino acids | Microbacterium natoriense | ? | - |
? | |
3.5.1.81 | additional information | no activity with N-acetyl-L-amino acids | Microbacterium natoriense TNJL143-2 | ? | - |
? | |
3.5.1.81 | N-acetyl-D-leucine + H2O | 59.9% of the activity with N-acetyl-D-phenylalanine | Microbacterium natoriense | acetate + D-leucine | - |
? | |
3.5.1.81 | N-acetyl-D-leucine + H2O | 59.9% of the activity with N-acetyl-D-phenylalanine | Microbacterium natoriense TNJL143-2 | acetate + D-leucine | - |
? | |
3.5.1.81 | N-acetyl-D-methionine + H2O | 25.1% of the activity with N-acetyl-D-phenylalanine | Microbacterium natoriense | acetate + D-methionine | - |
? | |
3.5.1.81 | N-acetyl-D-methionine + H2O | 25.1% of the activity with N-acetyl-D-phenylalanine | Microbacterium natoriense TNJL143-2 | acetate + D-methionine | - |
? | |
3.5.1.81 | N-acetyl-D-phenylalanine + H2O | - |
Microbacterium natoriense | acetate + D-phenylalanine | - |
? | |
3.5.1.81 | N-acetyl-D-phenylalanine + H2O | the enzyme purified from the cells of strain TNJL143-2 displays the highest preference for N-acetyl-D-phenylalanine | Microbacterium natoriense | acetate + D-phenylalanine | - |
? | |
3.5.1.81 | N-acetyl-D-phenylalanine + H2O | - |
Microbacterium natoriense TNJL143-2 | acetate + D-phenylalanine | - |
? | |
3.5.1.81 | N-acetyl-D-phenylalanine + H2O | the enzyme purified from the cells of strain TNJL143-2 displays the highest preference for N-acetyl-D-phenylalanine | Microbacterium natoriense TNJL143-2 | acetate + D-phenylalanine | - |
? | |
3.5.1.81 | N-acetyl-D-tryptophan + H2O | 14.4% of the activity with N-acetyl-D-phenylalanine | Microbacterium natoriense | acetate + D-tryptophan | - |
? | |
3.5.1.81 | N-acetyl-D-valine + H2O | 6.0% of the activity with N-acetyl-D-phenylalanine | Microbacterium natoriense | acetate + D-valine | - |
? | |
3.5.1.81 | N-acyl-D-amino acid + H2O | - |
Microbacterium natoriense | a carboxylate + D-amino acid | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
3.5.1.81 | monomer | 1 * 56000, SDS-PAGE | Microbacterium natoriense |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.81 | AcyM | - |
Microbacterium natoriense |
3.5.1.81 | DAA | - |
Microbacterium natoriense |
3.5.1.81 | N-Acyl-D-amino acid amidohydrolase | - |
Microbacterium natoriense |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.81 | 45 | - |
- |
Microbacterium natoriense |
EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.81 | 20 | 55 | activity range, profile overview | Microbacterium natoriense |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.5.1.81 | 20 | 45 | purified enzyme, over 60% activity remaining within this range | Microbacterium natoriense |
3.5.1.81 | 55 | - |
purified enzyme, inactivation | Microbacterium natoriense |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
3.5.1.81 | 41 | - |
N-acetyl-D-phenylalanine | pH 7.0, 37°C | Microbacterium natoriense |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.81 | 8 | 9 | - |
Microbacterium natoriense |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.81 | 6 | 10 | activity range, profile overview | Microbacterium natoriense |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
3.5.1.81 | 5 | 10 | purified enzyme, over 60% activity remaining within this range | Microbacterium natoriense |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
3.5.1.81 | 3 | 10 | pH 7.0, 37°C | Microbacterium natoriense | N-acetyl-D-phenylalanine |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.5.1.81 | evolution | 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 | Microbacterium natoriense |