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

1996; Portland Press; Volume: 320; Issue: 2 Linguagem: Inglês

10.1042/bj3200365

1470-8728

Nora Engel, Marı́a Teresa Olmo, Catherine S. Coleman, Miguel Ángel Medina, Anthony E. Pegg, Francisca Sánchez‐Jiménez,

Protein Hydrolysis and Bioactive Peptides

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 Km values for the respective substrates.