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Literature summary for 3.5.1.81 extracted from

  • Liu, J.; Asano, Y.; Ikoma, K.; Yamashita, S.; Hirose, Y.; Shimoyama, T.; Takahashi, S.; Nakayama, T.; Nishino, T.
    Purification, characterization, and primary structure of a novel N-acyl-D-amino acid amidohydrolase from Microbacterium natoriense TNJL143-2 (2012), J. Biosci. Bioeng., 114, 391-397.
    View publication on PubMed
Search for more literature for 3.5.1.81

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis Microbacterium natoriense

Inhibitors

Inhibitors Comment Organism Structure
CuCl2 93% inhibition at 1 mM Microbacterium natoriense
EDTA 35% inhibition at 20 mM, low inhibition level Microbacterium natoriense
HgCl2 99% inhibition at 1 mM Microbacterium natoriense
additional information no inhibition by 1 mM of by CaCl2, CoCl2, FeCl2, MnCl2, or CdCl2 Microbacterium natoriense
N-acetyl-D-phenylalanine substrate inhibition at high concentrations Microbacterium natoriense
ZnCl2 96% inhibition at 1 mM Microbacterium natoriense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Microbacterium natoriense
2.5
-
 N-acetyl-D-phenylalanine pH 7.0, 37°C Microbacterium natoriense

Metals/Ions

Metals/Ions Comment Organism Structure
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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
 1 * 56000, SDS-PAGE Microbacterium natoriense

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-acetyl-D-phenylalanine + H2O Microbacterium natoriense
-
 acetate + D-phenylalanine
-
 ?
N-acetyl-D-phenylalanine + H2O Microbacterium natoriense TNJL143-2
-
 acetate + D-phenylalanine
-
 ?
N-acyl-D-amino acid + H2O Microbacterium natoriense
-
 a carboxylate + D-amino acid
-
 ?

Organism

Organism UniProt Comment Textmining
Microbacterium natoriense I7HFV7
-
-
Microbacterium natoriense TNJL143-2 I7HFV7
-
-

Purification (Commentary)

Purification (Comment) Organism
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

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:N-acetyl-DL-phenylalanine-grown cell
-
 Microbacterium natoriense
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity with N-acetyl-L-amino acids Microbacterium natoriense ?
-
 ?
additional information no activity with N-acetyl-L-amino acids Microbacterium natoriense TNJL143-2 ?
-
 ?
N-acetyl-D-leucine + H2O 59.9% of the activity with N-acetyl-D-phenylalanine Microbacterium natoriense acetate + D-leucine
-
 ?
N-acetyl-D-leucine + H2O 59.9% of the activity with N-acetyl-D-phenylalanine Microbacterium natoriense TNJL143-2 acetate + D-leucine
-
 ?
N-acetyl-D-methionine + H2O 25.1% of the activity with N-acetyl-D-phenylalanine Microbacterium natoriense acetate + D-methionine
-
 ?
N-acetyl-D-methionine + H2O 25.1% of the activity with N-acetyl-D-phenylalanine Microbacterium natoriense TNJL143-2 acetate + D-methionine
-
 ?
N-acetyl-D-phenylalanine + H2O
-
 Microbacterium natoriense acetate + D-phenylalanine
-
 ?
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
-
 ?
N-acetyl-D-phenylalanine + H2O
-
 Microbacterium natoriense TNJL143-2 acetate + D-phenylalanine
-
 ?
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
-
 ?
N-acetyl-D-tryptophan + H2O 14.4% of the activity with N-acetyl-D-phenylalanine Microbacterium natoriense acetate + D-tryptophan
-
 ?
N-acetyl-D-valine + H2O 6.0% of the activity with N-acetyl-D-phenylalanine Microbacterium natoriense acetate + D-valine
-
 ?
N-acyl-D-amino acid + H2O
-
 Microbacterium natoriense a carboxylate + D-amino acid
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 56000, SDS-PAGE Microbacterium natoriense

Synonyms

Synonyms Comment Organism
AcyM
-
 Microbacterium natoriense
DAA
-
 Microbacterium natoriense
N-Acyl-D-amino acid amidohydrolase
-
 Microbacterium natoriense

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
-
 Microbacterium natoriense

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 55 activity range, profile overview Microbacterium natoriense

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 45 purified enzyme, over 60% activity remaining within this range Microbacterium natoriense
55
-
 purified enzyme, inactivation Microbacterium natoriense

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
41
-
 N-acetyl-D-phenylalanine pH 7.0, 37°C Microbacterium natoriense

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 9
-
 Microbacterium natoriense

pH Range

pH Minimum pH Maximum Comment Organism
6 10 activity range, profile overview Microbacterium natoriense

pH Stability

pH Stability pH Stability Maximum Comment Organism
5 10 purified enzyme, over 60% activity remaining within this range Microbacterium natoriense

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3 10 pH 7.0, 37°C Microbacterium natoriense N-acetyl-D-phenylalanine

General Information

General Information Comment Organism
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