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Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and
N Engel1, M T Olmo, C S Coleman
1Laboratorio de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Málaga, Spain.
The Biochemical Journal
|December 1, 1996
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.