Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase

Nora Engel, María Teresa Olmo, Catherine S. Coleman, Miguel Angel Medina, Anthony E. Pegg, Francisca Sánchez-Jiménez

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

Common protein motifs between histidine decarboxylase (HDC) and ornithine decarboxylase (ODC) were detected by computational analysis. Mutants were generated and expressed in vitro. In both enzymes, terminal PEST-region-containing fragments are not essential for decarboxylation (PEST regions are sequence fragments enriched in proline, glutamic acid, serine and threonine residues in a hydrophilic fragment flanked by cationic amino acids). The substitution of a very well conserved histidine residue by alanine causes a severalfold increase of the apparent K(m) values for the respective substrates.

Original languageEnglish (US)
Pages (from-to)365-368
Number of pages4
JournalBiochemical Journal
Volume320
Issue number2
DOIs
StatePublished - Dec 1 1996

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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