- About this Journal ·
- Abstracting and Indexing ·
- Advance Access ·
- Aims and Scope ·
- Annual Issues ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
BioMed Research International
Volume 2013 (2013), Article ID 161456, 10 pages
Interaction of Human Dopa Decarboxylase with L-Dopa: Spectroscopic and Kinetic Studies as a Function of pH
Section of Biological Chemistry, Department of Life Sciences and Reproduction, University of Verona, Strada Le Grazie 8, 37134 Verona, Italy
Received 18 April 2013; Accepted 8 May 2013
Academic Editor: Alessandro Paiardini
Copyright © 2013 Riccardo Montioli et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- A. Amadasi, M. Bertoldi, R. Contestabile et al., “Pyridoxal -phosphate enzymes as targets for therapeutic agents,” Current Medicinal Chemistry, vol. 14, no. 12, pp. 1291–1324, 2007.
- B. Cellini, A. Lorenzetto, R. Montioli, E. Oppici, and C. B. Voltattorni, “Human liver peroxisomal alanine:glyoxylate aminotransferase: different stability under chemical stress of the major allele, the minor allele, and its pathogenic G170R variant,” Biochimie, vol. 92, no. 12, pp. 1801–1811, 2010.
- B. Cellini, E. Oppici, A. Paiardini, and R. Montioli, “Molecular insights into primary hyperoxaluria type 1 pathogenesis,” Frontiers in Bioscience, vol. 17, pp. 621–634, 2012.
- M. L. di Salvo, R. Contestabile, A. Paiardini, and B. Maras, “Glycine consumption and mitochondrial serine hydroxymethyltransferase in cancer cells: the heme connection,” Medical Hypotheses, vol. 80, pp. 633–636, 2013.
- A. E. Pegg, L. M. Shantz, and C. S. Coleman, “Ornithine decarboxylase as a target for chemoprevention,” Journal of Cellular Biochemistry, vol. 58, no. 22, pp. 132–138, 1995.
- N. A. Rao, R. Talwar, and H. S. Savithri, “Molecular organization, catalytic mechanism and function of serine hydroxymethyltransferase—a potential target for cancer chemotherapy,” International Journal of Biochemistry and Cell Biology, vol. 32, no. 4, pp. 405–416, 2000.
- P. Storici, G. Capitani, D. De Biase et al., “Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy,” Biochemistry, vol. 38, no. 27, pp. 8628–8634, 1999.
- B. Cellini, R. Montioli, E. Oppici, and C. B. Voltattorni, “Biochemical and computational approaches to improve the clinical treatment of dopa decarboxylase-related diseases: an overview,” Open Biochemistry Journal, vol. 6, pp. 131–138, 2012.
- F. Daidone, R. Montioli, A. Paiardini, et al., “Identification by virtual screening and in vitro testing of human DOPA decarboxylase inhibitors,” PLoS ONE, vol. 7, no. 2, Article ID e31610, 2012.
- R. Montioli, E. Oppici, B. Cellini, A. Roncador, M. Dindo, and C. B. Voltattorni, “S250F variant associated with aromatic amino acid decarboxylase deficiency: molecular defects and intracellular rescue by pyridoxine,” Human Molecular Genetics, vol. 22, no. 8, pp. 1615–1624, 2013.
- R. Montioli, B. Cellini, and C. Borri Voltattorni, “Molecular insights into the pathogenicity of variants associated with the aromatic amino acid decarboxylase deficiency,” Journal of Inherited Metabolic Disease, vol. 34, pp. 1213–1224, 2011.
- B. Maras, P. Dominici, D. Barra, F. Bossa, and C. Borri Voltattorni, “Pig kidney 3,4-dihydroxyphenylalanine (Dopa) decarboxylase. Primary structure and relationships to other amino acid decarboxylases,” European Journal of Biochemistry, vol. 201, no. 2, pp. 385–391, 1991.
- C. B. Voltattorni, A. Minelli, and P. Dominici, “Interaction of aromatic amino acids in D and L forms with 3,4-dihydroxyphenylalanine decarboxylase from pig kidney,” Biochemistry, vol. 22, no. 9, pp. 2249–2254, 1983.
- C. B. Voltattorni, A. Minelli, and C. Turano, “Spectral properties of the coenzyme bound to DOPA decarboxylase from pig kidney,” FEBS Letters, vol. 17, no. 2, pp. 231–235, 1971.
- C. B. Voltattorni, A. Minelli, and P. Vecchini, “Purification and characterization of 3,4-dihydroxyphenylalanine decarboxylase from pig kidney,” European Journal of Biochemistry, vol. 93, no. 1, pp. 181–187, 1979.
- P. Dominici, B. Tancini, D. Barra, and C. B. Voltattorni, “Purification and characterization of rat-liver 3,4-dihydroxyphenylalanine decarboxylase,” European Journal of Biochemistry, vol. 169, no. 1, pp. 209–213, 1987.
- A. Fiori, C. Turano, and C. Borri Voltattorni, “Interaction of L DOPA decarboxylase with substrates. A spectrophotometric study,” FEBS Letters, vol. 54, no. 2, pp. 122–125, 1975.
- M. Bertoldi and C. Borri Voltattorni, “Reaction of dopa decarboxylase with L-aromatic amino acids under aerobic and anaerobic conditions,” Biochemical Journal, vol. 352, no. 2, pp. 533–538, 2000.
- M. Bertoldi, B. Cellini, B. Maras, and C. B. Voltattorni, “A quinonoid is an intermediate of oxidative deamination reaction catalyzed by Dopa decarboxylase,” FEBS Letters, vol. 579, no. 23, pp. 5175–5180, 2005.
- M. Bertoldi, B. Cellini, R. Montioli, and C. B. Voltattorni, “Insights into the mechanism of oxidative deamination catalyzed by DOPA decarboxylase,” Biochemistry, vol. 47, no. 27, pp. 7187–7195, 2008.
- M. Bertoldi, P. Frigeri, M. Paci, and C. B. Voltattorni, “Reaction specificity of native and nicked 3,4-dihydroxyphenylalanine decarboxylase,” Journal of Biological Chemistry, vol. 274, no. 9, pp. 5514–5521, 1999.
- M. Bertoldi, M. Gonsalvi, R. Contestabile, and C. B. Voltattorni, “Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase,” Journal of Biological Chemistry, vol. 277, no. 39, pp. 36357–36362, 2002.
- P. Dominici, P. S. Moore, S. Castellani, M. Bertoldi, and C. B. Voltattorni, “Mutation of cysteine 111 in Dopa decarboxylase leads to active site perturbation,” Protein Science, vol. 6, no. 9, pp. 2007–2015, 1997.
- P. S. Moore, P. Dominici, and C. Borri Voltattorni, “Cloning and expression of pig kidney dopa decarboxylase: comparison of the naturally occurring and recombinant enzymes,” Biochemical Journal, vol. 315, no. 1, pp. 249–256, 1996.
- H. Hayashi, H. Mizuguchi, and H. Kagamiyama, “Rat liver aromatic L-amino acid decarboxylase: spectroscopic and kinetic analysis of the coenzyme and reaction intermediates,” Biochemistry, vol. 32, no. 3, pp. 812–818, 1993.
- H. Hayashi, F. Tsukiyama, S. Ishii, H. Mizuguchi, and H. Kagamiyama, “Acid base chemistry of the reaction of aromatic L-amino acid decarboxylase and dopa analyzed by transient and steady-state kinetics: preferential binding of the substrate with its amino group unprotonated,” Biochemistry, vol. 38, no. 47, pp. 15615–15622, 1999.
- G. Giardina, R. Montioli, S. Gianni, et al., “Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 51, pp. 20514–20519, 2011.
- P. Burkhard, P. Dominici, C. Borri-Voltattorni, J. N. Jansonius, and V. N. Malashkevich, “Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase,” Nature Structural Biology, vol. 8, no. 11, pp. 963–967, 2001.
- R. Singh, F. Spyrakis, P. Cozzini, A. Paiardini, S. Pascarella, and A. Mozzarelli, “Chemogenomics of pyridoxal -phosphate dependent enzymes,” Journal of Enzyme Inhibition and Medicinal Chemistry, vol. 28, no. 1, pp. 183–194, 2013.
- A. Minelli, A. T. Charteris, C. B. Voltattorni, and R. A. John, “Reactions of DOPA (3,4-dihydroxyphenylalanine) decarboxylase with DOPA,” Biochemical Journal, vol. 183, no. 2, pp. 361–368, 1979.
- A. F. Sherald, J. C. Sparrow, and T. R. F. Wright, “A spectrophotometric assay for Drosophila dopa decarboxylase,” Analytical Biochemistry, vol. 56, no. 1, pp. 300–305, 1973.
- A. Charteris and R. John, “An investigation of the assay of dopamine using trinitrobenzensulphonic acid,” Analytical Biochemistry, vol. 66, no. 2, pp. 365–371, 1975.
- C. M. Metzler, A. G. Harris, and D. E. Metzler, “Spectroscopic studies of quinonoid species from pyridoxal 5'-phosphate,” Biochemistry, vol. 27, no. 13, pp. 4923–4933, 1988.
- M. Bertoldi and C. B. Voltattorni, “Multiple roles of the active site lysine of Dopa decarboxylase,” Archives of Biochemistry and Biophysics, vol. 488, no. 2, pp. 130–139, 2009.
- B. Cellini, M. Bertoldi, R. Montioli, and C. B. Voltattorni, “Probing the role of Tyr 64 of Treponema denticola cystalysin by site-directed mutagenesis and kinetic studies,” Biochemistry, vol. 44, no. 42, pp. 13970–13980, 2005.
- G. A. Hunter, J. Zhang, and G. C. Ferreira, “Transient kinetic studies support refinements to the chemical and kinetic mechanisms of aminolevulinate synthase,” Journal of Biological Chemistry, vol. 282, no. 32, pp. 23025–23035, 2007.
- X. Zhou and M. D. Toney, “pH Studies on the mechanism of the pyridoxal phosphate-dependent dialkylglycine decarboxylase,” Biochemistry, vol. 38, no. 1, pp. 311–320, 1999.
- W. E. Karsten, T. Ohshiro, Y. Izumi, and P. F. Cook, “Initial velocity, spectral, and pH studies of the serine-glyoxylate aminotransferase from Hyphomicrobiuim methylovorum,” Archives of Biochemistry and Biophysics, vol. 388, no. 2, pp. 267–275, 2001.
- D. M. Kiick and P. F. Cook, “pH studies toward the elucidation of the auxiliary catalyst for pig heart aspartate aminotransferase,” Biochemistry, vol. 22, no. 2, pp. 375–382, 1983.
- K. O. Honikel and N. B. Madsen, “Comparison of the absorbance spectra and fluorescence behavior of phosphorylase b with that of model pyridoxal phosphate derivatives in various solvents,” Journal of Biological Chemistry, vol. 247, no. 4, pp. 1057–1064, 1972.
- M. T. Olmo, F. Sánchez-Jiménez, M. A. Medina, and H. Hayashi, “Spectroscopic analysis of recombinant rat histidine decarboxylase,” Journal of Biochemistry, vol. 132, no. 3, pp. 433–439, 2002.
- W. C. Chu and D. E. Metzler, “Enzymatically active truncated cat brain glutamate decarboxylase: expression, purification, and absorption spectrum,” Archives of Biochemistry and Biophysics, vol. 313, no. 2, pp. 287–295, 1994.