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Literature summary for 4.1.1.28 extracted from

  • Giardina, G.; Montioli, R.; Gianni, S.; Cellini, B.; Paiardini, A.; Voltattorni, C.B.; Cutruzzola, F.
    Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases (2011), Proc. Natl. Acad. Sci. USA, 108, 20514-20519.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
apoenzyme, to 2.9 A resolution. The apoenzyme exists in an unexpected open conformation. Compared to the pig kidney holoenzyme, the dimer subunits move 20 A apart and the two active sites become solvent exposed. Complete achievement of the closed conformation of the dimer is not essential for Schiff base formation and pyridoxal 5'-phosphate binding to the intermediate monomer is able to induce rearrangement of loop1. Covalent binding of the cofactor can only be achieved after an initial rearrangement towards the closed conformation Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P20711
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