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Literature summary for 4.1.1.28 extracted from

  • Montioli, R.; Cellini, B.; Dindo, M.; Oppici, E.; Voltattorni, C.
    Interaction of human Dopa decarboxylase with L-dopa: Spectroscopic and kinetic studies as a function of pH (2013), BioMed Res. Int., 2013, 161456.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3,4-Dihydroxyphenylalanine during the reaction with L-Dopa, monitored by stopped-flow spectrophotometry, a 420 nm band attributed to the 4'-N-protonated external aldimine first appears, and its decrease parallels the emergence of a 390 nm peak, assigned to the 4'-N-unprotonated external aldimine. The pH profile of the spectral change at 390 nm displays a pK of 6.4, which may represent the ESH(+) -> ES catalytic step Homo sapiens Dopamine + CO2
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