Structure/function relationship studies on the T/S residues 173-177 of rat ODC

José Manuel Matés, Alicia E. Del Valle, José Luis Urdiales, Catherine Coleman, David Feith, M. Teresa Olmo, Anthony Pegg, Francisca Sánchez-Jiménez

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

A well-conserved T/S cluster was detected among vertebrate ornithine decarboxylase by computer analysis (E. Viguera, O. Trelles, J.L. Urdiales, J.M. Mates, F. Sanchez-Jimenez, Trends Biochem. Sci. 19 (1994) 318-319). In the present report we studied the role of these residues (173, 176 and 177 in rat ornithine decarboxylase (ODC)) in enzymic activity and stability by in vitro expression, kinetic characterization and in vitro degradation of site-directed mutants. These T/S residues are substituted by a D/E-enriched fragment in other lower eukaryotic ODCs. The substitution of the T/S-enriched fragment (TLKTS) of rat ODC by the negative charged fragment of T. brucei ODC (KVEDC) did not affect protein stability, but increased K(m) values of the mutant enzyme. The substitution of the T/S residues by alanine also has a similar effect on rat ODC kinetic values. However, results indicate that polarity of the fragment must be an important factor for protein conformation, since the latter mutant, having no T/S or D/E residue in the fragment (ALKAA), showed reduced stability in vitro. Copyright (C) 1998 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)113-120
Number of pages8
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume1386
Issue number1
DOIs
StatePublished - Jul 28 1998

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Ornithine Decarboxylase
Rats
Substitution reactions
Protein Conformation
Kinetics
Protein Stability
Alanine
Conformations
Vertebrates
Proteins
Degradation
Enzymes
In Vitro Techniques

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Structural Biology
  • Biophysics

Cite this

Matés, J. M., Del Valle, A. E., Urdiales, J. L., Coleman, C., Feith, D., Olmo, M. T., ... Sánchez-Jiménez, F. (1998). Structure/function relationship studies on the T/S residues 173-177 of rat ODC. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 1386(1), 113-120. https://doi.org/10.1016/S0167-4838(98)00090-9
Matés, José Manuel ; Del Valle, Alicia E. ; Urdiales, José Luis ; Coleman, Catherine ; Feith, David ; Olmo, M. Teresa ; Pegg, Anthony ; Sánchez-Jiménez, Francisca. / Structure/function relationship studies on the T/S residues 173-177 of rat ODC. In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology. 1998 ; Vol. 1386, No. 1. pp. 113-120.
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Matés, JM, Del Valle, AE, Urdiales, JL, Coleman, C, Feith, D, Olmo, MT, Pegg, A & Sánchez-Jiménez, F 1998, 'Structure/function relationship studies on the T/S residues 173-177 of rat ODC', Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, vol. 1386, no. 1, pp. 113-120. https://doi.org/10.1016/S0167-4838(98)00090-9

Structure/function relationship studies on the T/S residues 173-177 of rat ODC. / Matés, José Manuel; Del Valle, Alicia E.; Urdiales, José Luis; Coleman, Catherine; Feith, David; Olmo, M. Teresa; Pegg, Anthony; Sánchez-Jiménez, Francisca.

In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1386, No. 1, 28.07.1998, p. 113-120.

Research output: Contribution to journalArticle

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T1 - Structure/function relationship studies on the T/S residues 173-177 of rat ODC

AU - Matés, José Manuel

AU - Del Valle, Alicia E.

AU - Urdiales, José Luis

AU - Coleman, Catherine

AU - Feith, David

AU - Olmo, M. Teresa

AU - Pegg, Anthony

AU - Sánchez-Jiménez, Francisca

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Y1 - 1998/7/28

N2 - A well-conserved T/S cluster was detected among vertebrate ornithine decarboxylase by computer analysis (E. Viguera, O. Trelles, J.L. Urdiales, J.M. Mates, F. Sanchez-Jimenez, Trends Biochem. Sci. 19 (1994) 318-319). In the present report we studied the role of these residues (173, 176 and 177 in rat ornithine decarboxylase (ODC)) in enzymic activity and stability by in vitro expression, kinetic characterization and in vitro degradation of site-directed mutants. These T/S residues are substituted by a D/E-enriched fragment in other lower eukaryotic ODCs. The substitution of the T/S-enriched fragment (TLKTS) of rat ODC by the negative charged fragment of T. brucei ODC (KVEDC) did not affect protein stability, but increased K(m) values of the mutant enzyme. The substitution of the T/S residues by alanine also has a similar effect on rat ODC kinetic values. However, results indicate that polarity of the fragment must be an important factor for protein conformation, since the latter mutant, having no T/S or D/E residue in the fragment (ALKAA), showed reduced stability in vitro. Copyright (C) 1998 Elsevier Science B.V.

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