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Literature summary for 3.4.11.19 extracted from

  • Yamaguchi, S.; Komeda, H.; Asano, Y.
    New enzymatic method of chiral amino acid synthesis by dynamic kinetic resolution of amino acid amides: use of stereoselective amino acid amidases in the presence of alpha-amino-epsilon-caprolactam racemase (2007), Appl. Environ. Microbiol., 73, 5370-5373.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
pyridoxal 5'-phosphate
-
Brucella anthropi

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Brucella anthropi

Organism

Organism UniProt Comment Textmining
Brucella anthropi
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-2-aminobutyric amide + H2O in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae Brucella anthropi D-2-aminobutyric acid + NH3
-
?
L-alanine amide + H2O in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae Brucella anthropi D-alanine + NH3
-
?
L-methionine amide + H2O in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae Brucella anthropi D-methionine + NH3
-
?
L-serine amide + H2O in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae Brucella anthropi D-serine + NH3
-
?

Synonyms

Synonyms Comment Organism
D-aminopeptidase
-
Brucella anthropi
DAP
-
Brucella anthropi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
Brucella anthropi

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
at 50°C the rate of conversion is decreased because of the instability of DAP at higher temperatures Brucella anthropi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
Brucella anthropi