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Literature summary for 5.1.1.15 extracted from
- 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.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| ACL racemase from Achromobacter obae is expressed in Escherichia coli, 300 U/liter culture | Achromobacter obae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Achromobacter obae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| ACL racemase is purified from Escherichia coli JM109/pACL60 | Achromobacter obae |
Reaction
| 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
| 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 |
|---|---|---|---|
| 45 | - |
maximum conversion rate | Achromobacter obae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
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
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | - |
Achromobacter obae | |
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