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Article

Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Effects on catalytic properties.

European journal of biochemistry - 1 May 2001

Bertoldi M, Castellani S, Bori Voltattorni C

Abstract excerpt

Residues D271, H192, H302 and N300 of L-3,4-dihydroxyphenylalanine decarboxylase (DDC), a homodimeric pyridoxal 5'-phosphate (PLP) enzyme, were mutated in order to acquire information on the catalytic mechanism. These residues are potential participants in catalysis because they belong to the common PLP-binding structural motif of group I, II and III decarboxylases and other PLP enzymes, and because they are...

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Source

Identifiers

PMID: 11358515
DOI: 10.1046/j.1432-1327.2001.02187.x

Genes

DDC

Variants

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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