EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.5.1.11 | C290C | 20% decrease in production of penicillin G acylase activity | Escherichia coli |
3.5.1.11 | F146L | mutation in alpha-subunit,3fold increase in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile | Escherichia coli |
3.5.1.11 | F146W | mutation in alpha-subunit, 40fold decrease in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile | Escherichia coli |
3.5.1.11 | F146Y | mutation in alpha-subunit, 40fold decrease in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile | Escherichia coli |
3.5.1.11 | F24A | mutation in beta-subunit, 3fold increase in transferase/hydrolase ratio using 6-aminopenicillanic acid as nucleophile | Escherichia coli |
3.5.1.11 | F24A | mutation in the beta-subunit produces a protein with a higher synthesis/hydrolysis ratio, increased acylase activity, and more resistance to inhibition by phenyl acetic acid | Escherichia coli |
3.5.1.11 | F71C | mutation in B-subunit shows a 100fold increase in kcat/Km towards glutaryl-L-leucine | Escherichia coli |
3.5.1.11 | F71L | mutation in B-subunit shows a 100fold increase in kcat/Km towards glutaryl-L-leucine | Escherichia coli |
3.5.1.11 | K299H | mutant shows very low processing and 90% loss of activity | Escherichia coli |
3.5.1.11 | K299Q | mutant enzyme shows no processing | Escherichia coli |
3.5.1.11 | K299S | mutant enzyme shows no processing | Escherichia coli |
3.5.1.11 | K427A | mutation in beta-chain. Half-life is improved by 60% compared to wild-type enzyme | Priestia megaterium |
3.5.1.11 | K427A | mutation in beta-chain. Mutant shows a great stability to organic solvents | Priestia megaterium |
3.5.1.11 | K430A | mutation in beta-chain. Half-life is improved by 166% compared to wild-type enzyme | Priestia megaterium |
3.5.1.11 | K430A | mutation in beta-chain. Mutant shows a good stability to solvent and thermostability | Priestia megaterium |
3.5.1.11 | K430A/K427A | mutation in beta-chain. Mutant shows a good stability to solvent and thermostability | Priestia megaterium |
3.5.1.11 | additional information | transversion mutation of thymine to guanine at position 1163 results in 90% and 50% of activity loss in penicillin G acylase activity on penicillin G and phenylacetyl-L-leucine respectively | Kluyvera cryocrescens |
3.5.1.11 | T289C | production of penicillin G acylase activity is 92% improved | Escherichia coli |
3.5.1.11 | T289G | production of penicillin G acylase activity is 20% improved | Escherichia coli |
3.5.1.11 | T289S | production of penicillin G acylase activity is 85% improved | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.11 | Escherichia coli | - |
- |
- |
3.5.1.11 | Kluyvera cryocrescens | - |
- |
- |
3.5.1.11 | Priestia megaterium | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.5.1.11 | penicillin G + H2O | - |
Kluyvera cryocrescens | 6-aminopenicillanic acid + phenylacetic acid | - |
? | |
3.5.1.11 | phenylacetyl-L-leucine + H2O | - |
Kluyvera cryocrescens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.11 | penicillin G acylase | - |
Escherichia coli |
3.5.1.11 | penicillin G acylase | - |
Priestia megaterium |
3.5.1.11 | penicillin G acylase | - |
Kluyvera cryocrescens |