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Literature summary extracted from

  • Chen, C.X.; Jiang, B.; Branford-White, C.; Zhu, L.M.
    Enantioselective reductive amination of alpha-keto acids by papain-based semisynthetic enzyme (2009), Biochemistry (Moscow), 74, 36-40.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.22.2 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

EC Number Organism UniProt Comment Textmining
3.4.22.2 Carica papaya
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