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Literature summary for 3.5.1.81 extracted from

  • Kumagai, S.; Kobayashi, M.; Yamaguchi, S.; Kanaya, T.; Motohashi, R.; Isobe, K.
    A new D-aminoacylase from Defluvibacter sp. A 131-3 (2004), J. Mol. Catal. B, 30, 159-165.
No PubMed abstract available
Search for more literature for 3.5.1.81

Application

Application Comment Organism
synthesis the enzyme can be useful in production of D-valine Defluvibacter sp.

Inhibitors

Inhibitors Comment Organism Structure
CoCl2
-
 Defluvibacter sp.
MnCl2
-
 Defluvibacter sp.
NiCl2
-
 Defluvibacter sp.
ZnCl2
-
 Defluvibacter sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
 1 * 56000 Defluvibacter sp.

Organism

Organism UniProt Comment Textmining
Defluvibacter sp.
-
-
-
Defluvibacter sp. A 131-3
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme to homogeneity Defluvibacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-D-valine + H2O preferred substrate, the enzyme is specific for N-acyl-D-amino acids Defluvibacter sp. acetate + D-valine
-
 ?
N-acetyl-D-valine + H2O preferred substrate, the enzyme is specific for N-acyl-D-amino acids Defluvibacter sp. A 131-3 acetate + D-valine
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 56000 Defluvibacter sp.

Synonyms

Synonyms Comment Organism
D-Aminoacylase
-
 Defluvibacter sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
 Defluvibacter sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Defluvibacter sp.

pI Value

Organism Comment pI Value Maximum pI Value
Defluvibacter sp.
-
-
 5.3