Application | Comment | Organism |
---|---|---|
synthesis | penicillin amidase from Alacaligenes faecalis is an attractive biocatalyst for hydrolysis of penicillin G for production of 6-aminopenicillanic acid, which is used in the synthesis of semi-synthetic beta-lactam antibiotics | Alcaligenes faecalis |
Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli BL21(DE3) | Alcaligenes faecalis |
Protein Variants | Comment | Organism |
---|---|---|
T206G/S213G | construction of a mutant with extended C-terminus of the A-chain comprising parts of the connecting linker peptide showing almost 2fold increased activity and 3fold higher specificity compared to the wild-type enzyme, overview | Alcaligenes faecalis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
penicillin G + H2O | Alcaligenes faecalis | - |
phenylacetic acid + 6-aminopenicillanate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Alcaligenes faecalis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli BL21(DE3) to homogeneity | Alcaligenes faecalis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
80 | - |
wild-type enzyme, pH 7.5, 25°C | Alcaligenes faecalis |
140 | - |
T206G/S213G mutant enzyme, pH 7.5, 25°C | Alcaligenes faecalis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
penicillin G + H2O | - |
Alcaligenes faecalis | phenylacetic acid + 6-aminopenicillanate | - |
? | |
penicillin G + H2O | - |
Alcaligenes faecalis | phenylacetic acid + 6-aminopenicillanate | product detection by reaction with substrate 6-nitro-3-(phenylacetamido)benzoic acid | ? |
Synonyms | Comment | Organism |
---|---|---|
penicillin amidase | belongs to the family of N-terminal nucleophile hydrolases acting on carbon nitrogen bonds in linear amides | Alcaligenes faecalis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Alcaligenes faecalis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
15 | 95 | temperature-induced unfolding studies of recombinant wild-type and mutant enzymes, kinetics, overview | Alcaligenes faecalis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Alcaligenes faecalis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
3.9 | 10.7 | pH-stability studies of recombinant wild-type and mutant enzymes, inactivation above pH 10.7 and below pH 3.9, overview | Alcaligenes faecalis |