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Literature summary 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.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.19 | pyridoxal 5'-phosphate | - |
Brucella anthropi |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.19 | expressed in Escherichia coli | Brucella anthropi |
| 5.1.1.15 | ACL racemase from Achromobacter obae is expressed in Escherichia coli, 300 U/liter culture | Achromobacter obae |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.19 | Brucella anthropi | - |
- |
- |
| 5.1.1.15 | Achromobacter obae | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.15 | ACL racemase is purified from Escherichia coli JM109/pACL60 | Achromobacter obae |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.1.1.15 | (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]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.15 | additional information | - |
300 U/liter culture | Achromobacter obae |
| 5.1.1.15 | 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)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.19 | L-2-aminobutyric amide + H2O | in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae | Brucella anthropi | D-2-aminobutyric acid + NH3 | - |
? | |
| 3.4.11.19 | L-alanine amide + H2O | in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae | Brucella anthropi | D-alanine + NH3 | - |
? | |
| 3.4.11.19 | L-methionine amide + H2O | in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae | Brucella anthropi | D-methionine + NH3 | - |
? | |
| 3.4.11.19 | L-serine amide + H2O | in the presence of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae | Brucella anthropi | D-serine + NH3 | - |
? | |
| 5.1.1.15 | L-alanine amide | - |
Achromobacter obae | D-alanine amide | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.19 | D-aminopeptidase | - |
Brucella anthropi |
| 3.4.11.19 | DAP | - |
Brucella anthropi |
| 5.1.1.15 | ACL racemase | - |
Achromobacter obae |
| 5.1.1.15 | alpha-Amino-epsilon-caprolactam racemase | - |
Achromobacter obae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.19 | 30 | - |
- |
Brucella anthropi |
| 5.1.1.15 | 45 | - |
maximum conversion rate | Achromobacter obae |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.19 | 50 | - |
at 50°C the rate of conversion is decreased because of the instability of DAP at higher temperatures | Brucella anthropi |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.19 | 7.3 | - |
- |
Brucella anthropi |
| 5.1.1.15 | 7.5 | - |
highest conversion | Achromobacter obae |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.1.15 | 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
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.15 | pyridoxal 5'-phosphate | - |
Achromobacter obae | |
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Release 2023.1 (January 2023)
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