Abstract
Urocanase catalyzes the second step in the degradation of histidine (Fig. 1). The reaction comprises a net addition of water to urocanic acid and can be formulated as a 1,4-addition to an activated diene system, followed by several tautomerizations. As a final result the imidazole ring is oxidized while the side-chain double bond is reduced. One drawback of this mechanism is the difficulty of a nucleophilic attack on the electron-rich imidazole ring.
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© 1981 Springer-Verlag Berlin Heidelberg
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Gerlinger, E., Hull, W.E., Rétey, J. (1981). Studies of the Mechanism of Action of Urocanase. In: Eggerer, H., Huber, R. (eds) Structural and Functional Aspects of Enzyme Catalysis. Colloquium der Gesellschaft für Biologische Chemie 23.–25. April 1981 in Mosbach/Baden, vol 32. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81738-0_18
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DOI: https://doi.org/10.1007/978-3-642-81738-0_18
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