title: Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase.
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.
authors.affiliation: Laboratorio de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Málaga, Spain.
authors.forename: N
authors.initials: N
authors.lastname: Engel
authors.forename: M T
authors.initials: MT
authors.lastname: Olmo
authors.forename: C S
authors.initials: CS
authors.lastname: Coleman
authors.forename: M A
authors.initials: MA
authors.lastname: Medina
authors.forename: A E
authors.initials: AE
authors.lastname: Pegg
authors.forename: F
authors.initials: F
authors.lastname: Sánchez-Jiménez
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017931:DNA Primers; D005333:Fetus; D006640:Histidine Decarboxylase / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008322:Mammals; D051379:Mice; D009955:Ornithine Decarboxylase / Q000096:biosynthesis / Q000737:chemistry* / Q000378:metabolism*; D016133:Polymerase Chain Reaction; D051381:Rats; D017208:Rats, Wistar; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D017384:Sequence Deletion
chemical_list: D017931:DNA Primers; D011994:Recombinant Proteins; D009955:Ornithine Decarboxylase; D006640:Histidine Decarboxylase