Any feedback?
Please rate this page

BRENDA support

Literature summary for 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


Cloned (Comment) Organism
ACL racemase from Achromobacter obae is expressed in Escherichia coli, 300 U/liter culture Achromobacter obae


Organism UniProt Comment Textmining
Achromobacter obae

Purification (Commentary)

Purification (Comment) Organism
ACL racemase is purified from Escherichia coli JM109/pACL60 Achromobacter obae


Reaction Comment Organism Reaction ID
(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam D- and L-amino acids are produced from L- and D-amino acid amides by D-aminopeptidase from Ochrobactrum anthropi C1-38 and L-amino acid amidase from Pseudomonas azotoformans IAM 1603, respectively, in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae. Substrate: L-alanine amide, product: D-alanine (100% yield), substrate: L-2-aminobutyric amide, product: D-2-aminobutyric acid (100% yield), substrate: L-serine amide, product: D-serine (94% yield), substrate: L-methionine amide, product: D-methionine (100% yield), substrate: D-alanine amide, product: L-alanine (100% yield), substrate: D-leucine amide, product: L-leucine (100% yield), substrate: D-methionine amide, product: L-methionine (100% yield) Achromobacter obae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
300 U/liter culture Achromobacter obae
additional information
the effect of the concentration of L-alanine amide on the racemization reaction catalyzed by ACL racemase is investigated. Formation of D-alanine amide increases when the concentration of L-alanine amide is increased from 0.6 M to 1.2 M, indicating that the enzyme activity is not inhibited by the high substrate concentration Achromobacter obae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-alanine amide
Achromobacter obae D-alanine amide


Synonyms Comment Organism
ACL racemase
Achromobacter obae
alpha-Amino-epsilon-caprolactam racemase
Achromobacter obae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
maximum conversion rate Achromobacter obae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
highest conversion Achromobacter obae

pH Range

pH Minimum pH Maximum Comment Organism
6.5 9.2 the effect of pH on D- or L-alanine production from L- or D-alanine amide with D-aminopeptidase or L-Aminoacid amide hydrolase in the presence of ACL racemase is investigated. Racemization is performed by ACL racemase at pH values of 6.5 to 9.2, and the maximum rate of conversion is found at pH 7.5 and at a temperature of around 45°C Achromobacter obae


Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
Achromobacter obae