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.
Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase
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Nora ENGEL, María Teresa OLMO, Catherine S. COLEMAN, Miguel Angel MEDINA, Anthony E. PEGG, Francisca SÁNCHEZ-JIMÉNEZ; Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase. Biochem J 1 December 1996; 320 (2): 365–368. doi: https://doi.org/10.1042/bj3200365
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