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Literature summary for 3.4.22.2 extracted from
- Enantioselective reductive amination of alpha-keto acids by papain-based semisynthetic enzyme (2009), Biochemistry (Moscow), 74, 36-40.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | alkylation of a cysteine residue in papain with a pyridoxamine results in a semi-synthetic enzyme papain-PX that has no detectable protease activity but has the ability to catalyze enantioselective reductive amination of alpha-keto acids such as alpha-ketoglutarate and pyruvate. Papain-PX reductively aminates the alkyl side chain of functionalized alpha-keto acids to give the respective alpha-amino acids with enantioselectivities greater than 70% | Carica papaya |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Carica papaya | - |
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Release 2023.1 (January 2023)
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