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

doi:10.1042/bj3200365

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 journal › Article › peer-review

32 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 language	English (US)
Pages (from-to)	365-368
Number of pages	4
Journal	Biochemical Journal
Volume	320
Issue number	2
DOIs	https://doi.org/10.1042/bj3200365
State	Published - Dec 1 1996

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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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.",

author = "Nora Engel and Olmo, {Mar{\'i}a Teresa} and Coleman, {Catherine S.} and Medina, {Miguel Angel} and Pegg, {Anthony E.} and Francisca S{\'a}nchez-Jim{\'e}nez",

year = "1996",

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T1 - Experimental evidence for structure-activity features in common between mammalian histidine decarboxylase and ornithine decarboxylase

AU - Engel, Nora

AU - Olmo, María Teresa

AU - Coleman, Catherine S.

AU - Medina, Miguel Angel

AU - Pegg, Anthony E.

AU - Sánchez-Jiménez, Francisca

PY - 1996/12/1

Y1 - 1996/12/1

N2 - 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.

AB - 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.

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

Abstract

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