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Literature summary for 5.4.3.11 extracted from

  • Wu, B.; Szymanski, W.; Wybenga, G.; Heberling, M.; Bartsch, S.; Dewildeman, S.; Poelarends, G.; Feringa, B.; Dijkstra, B.; Janssen, D.
    Mechanism-inspired engineering of phenylalanine aminomutase for enhanced beta-regioselective asymmetric amination of cinnamates (2012), Angew. Chem. Int. Ed. Engl., 51, 482-486.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
4-methylideneimidazole-5-one
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Taxus chinensis

Organism

Organism UniProt Comment Textmining
Taxus chinensis Q68G84
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine
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Taxus chinensis L-beta-phenylalanine when L-Phe enters the active site, the carboxylate group forms a bidentate salt bridge with residue R325. The carboxylate group further interacts with residue Q319. The amine group and the pro-3S hydrogen atom are oriented in an anti-periplanar geometry suitable for the elimination step. A nucleophilic attack of the amine group of the substrate on the 4-methylideneimidazole-5-one cofactor group preceeds abstraction of the proton by the general base Y80, possibly assisted by another basic group, and elimination of 4-methylideneimidazole-5-one-NH2. This leads to formation of trans-cinnamic acid, with the carboxylate group still bound to residue R325. The next step is the readdition of 4-methylideneimidazole-5-one-NH2 to the beta-position and of the proton to the alpha-position. This step requires exposure of the Re face of Cbeta to the 4-methylideneimidazole-5-one-NH2 and the carboxylate group to function as a good electron sink r
additional information enzyme additionally displays ammonia lyase activity, EC. 4.3.1.24, catalyzing the elimination of ammonia from L-phenylalanine to give trans-cinnamate Taxus chinensis ?
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