Any feedback?
Literature summary for 3.4.21.62 extracted from
- Improved enantioselectivity of subtilisin Carlsberg towards secondary alcohols by protein engineering (2018), ChemBioChem, 19, 338-346 .
Application
| Application | Comment | Organism |
|---|---|---|
| detergent | the enzyme subtilisin Carlsberg is industrially applied as an ingredient in various detergent products | Bacillus licheniformis |
| synthesis | the enzyme subtilisin Carlsberg (SC) is industrially applied or synthetic organic chemistry applications, it has been used to enrich the S enantiomer of a racemic alcohol mixture by dynamic kinetic resolution (DKR) systems by combining SC with a ruthenium complex in organic solvent | Bacillus licheniformis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G165L | site-directed mutagenesis, the mutant shows slightly increased transacylation activity compared to wild-type | Bacillus licheniformis |
| G165L/M221C | site-directed mutagenesis, the mutant shows about 5fold increased transacylation activity compared to wild-type | Bacillus licheniformis |
| G165L/M221F | site-directed mutagenesis, the mutant shows about 6.5fold increased transacylation activity compared to wild-type | Bacillus licheniformis |
| G165L/M221S | site-directed mutagenesis, the mutant shows slightly increased transacylation activity compared to wild-type | Bacillus licheniformis |
| M221A | site-directed mutagenesis, the mutant shows reduced transacylation activity compared to wild-type | Bacillus licheniformis |
| M221C | site-directed mutagenesis, the mutant shows similar transacylation activity compared to wild-type | Bacillus licheniformis |
| M221F | site-directed mutagenesis, the mutant shows similar transacylation activity compared to wild-type | Bacillus licheniformis |
| M221S | site-directed mutagenesis, the mutant shows unaltered transacylation activity compared to wild-type | Bacillus licheniformis |
| M221W | site-directed mutagenesis, the mutant shows reduced transacylation activity compared to wild-type | Bacillus licheniformis |
| additional information | immobilization of recombinant subtilisin Carlsberg. Enantioselectivities of immobilized wild-type and mutants of subtilisin Carlsberg in the transacylation of racemic 1-phenylethanol and vinyl butyrate in tetrahydrofuran | Bacillus licheniformis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Bacillus licheniformis | - |
- |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus licheniformis | P00780 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 rac-1-(4-chlorophenyl)ethan-1-ol + vinyl butyrate | - |
Bacillus licheniformis | (1S)-1-(4-chlorophenyl)ethyl butyrate + (1R)-1-(4-chlorophenyl)ethan-1-ol + ? | - |
? |  |
| 2 rac-1-(4-methoxyphenyl)ethan-1-ol + vinyl butyrate | substrate only of mutant G165L/M221F, not of the wild-type enzyme | Bacillus licheniformis | (1S)-1-(4-methoxyphenyl)ethyl butyrate + (1R)-1-(4-methoxyphenyl)ethan-1-ol + ? | - |
? | |
| 2 rac-1-(4-methylphenyl)ethan-1-ol + vinyl butyrate | substrate only of mutant G165L/M221F, not of the wild-type enzyme | Bacillus licheniformis | (1S)-1-(4-methylphenyl)ethyl butyrate + (1R)-1-(4-methylphenyl)ethan-1-ol + ? | - |
? | |
| 2 rac-1-phenylbutan-1-ol + vinyl butyrate | substrate only of mutant G165L/M221F, not of the wild-type enzyme | Bacillus licheniformis | (S)-1-phenylbutyl butyrate + (R)-1-phenylbutan-1-ol + ? | - |
? | |
| 2 rac-1-phenylethanol + vinyl butyrate | - |
Bacillus licheniformis | (S)-1-phenylethyl butyrate + (R)-1-phenylethanol + ? | - |
? | |
| 2 rac-1-phenylheptan-1-ol + vinyl butyrate | substrate only of mutant G165L/M221F, not of the wild-type enzyme | Bacillus licheniformis | (S)-1-phenylheptyl butyrate + (R)-1-phenylheptan-1-ol + ? | - |
? | |
| 2 rac-1-phenylpentan-1-ol + vinyl butyrate | substrate only of mutant G165L/M221F, not of the wild-type enzyme | Bacillus licheniformis | (S)-1-phenylpentyl butyrate + (R)-1-phenylpentan-1-ol + ? | - |
? | |
| 2 rac-1-phenylpropan-1-ol + vinyl butyrate | substrate only of mutant G165L/M221F, not of the wild-type enzyme | Bacillus licheniformis | (S)-1-phenylpropyl butyrate + (R)-1-phenylpropan-1-ol + ? | - |
? | |
| additional information | low catalytic activity of subtilisin Carlsberg (SC) for transacylation reactions with secondary alcohols in organic solvent, tetrahedral intermediates of the model reaction, enzyme with bound (S)-alpha-methylbenzyl butyrate or (R)-alpha-methylbenzyl butyrate, overview. The alkyl chain of the acyl donor, vinyl butyrate, is coordinated into the S1 binding pocket. The alkyl chain of the secondary alcohol is directed into the S1' binding pocket, and the phenyl group is directed towards the solvent. G165 is located in the bottom of the S1 pocket. Enantioselectivities of immobilized wild-type and mutants of subtilisin Carlsberg in the transacylation of racemic 1-phenylethanol and vinyl butyrate in tetrahydrofuran. Molecular modeling | Bacillus licheniformis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| subC | - |
Bacillus licheniformis |
| subtilisin Carlsberg | - |
Bacillus licheniformis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 23 | 25 | transacylation reaction at | Bacillus licheniformis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.8 | - |
transacylation reaction at | Bacillus licheniformis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | subtilisin Carlsberg is a serine protease naturally secreted from Bacillus licheniformis | Bacillus licheniformis |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
