Spectroscopic analysis of recombinant rat histidine decarboxylase

Journal of Biochemistry

Volumn 132, Issue 3, 2002, Pages 433-439

  Olmo, María Teresa ^a   Sánchez Jiménez, Francisca ^a   Medina, Miguel Angel ^a   Hayashi, Hideyuki ^b  

^a UNIVERSITY OF MÁLAGA   (Spain)

^b OSAKA MEDICAL COLLEGE   (Japan)

Author keywords

Catalytic mechanism; Histamine; Histidine decarboxylase; Pyridoxal 5 5 phosphate dependent enzyme

Indexed keywords

HISTIDINE DECARBOXYLASE; PRIMER DNA; RECOMBINANT PROTEIN; AMINO ACID DECARBOXYLASE; HISTAMINE; PYRIDOXAL 5 PHOSPHATE; RECOMBINANT ENZYME;

ANIMAL; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; RAT; SPECTROFLUOROMETRY; ABSORPTION SPECTROPHOTOMETRY; CATALYSIS; ENZYME ACTIVITY; ENZYME PURIFICATION; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; NONHUMAN; RECOMBINANT PLASMID; SPECTROPHOTOMETRY;

ANIMALS; BASE SEQUENCE; CIRCULAR DICHROISM; DNA PRIMERS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; HISTIDINE DECARBOXYLASE; RATS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE;

ESCHERICHIA COLI; MAMMALIA; PROKARYOTA;

EID: 0036737948     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a003240     Document Type: Article

References (36)

1. Sandmeier, E., Hale, T.I., and Christen, P. (1994) Multiple evolutionary origin of pyridoxal-5′-phosphate-dependent amino acid decarboxylases. Eur. J. Biochem. 221, 997-1002
2. Jansonius, J.N. (1998) Structure, evolution and action of vitamin B6-dependent enzymes. Curr. Opin. Struct. Biol. 8, 759-769
3. Momany, C., Ernst, S., Ghosh, R., Chang, N.L., and Hackert, M.L. (1995) Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 Å resolution. J. Mol. Biol. 252, 643-655
4. Kern, A.D., Oliveira, M.A., Coffino, P., and Hackert, M.L. (1999) Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Structure 7, 567-581
5. Kern, A., Oliveira, M.A., Chang, N.L., Ernst, S.R., Carroll, D.W., Momany, C., Minard, K., Coffino, P., and Hackert, M.L. (1996) Crystallization of a mammalian ornithine decarboxylase. Proteins 24, 266-268
6. Burkhard, P., Dominici, P., Borri-Voltattorni, C., Jansonius, J.N., and Malashkevich, V.N. (2001) Structural insight into Parkinson's disease treatment from drug-inhibited DOPA decarboxylase. Nat. Struct. Biol. 8, 963-967
7. Dunathan, H.C. and Voet, J.G. (1974) Stereochemical evidence for the evolution of pyridoxal-phsphate enzymes of various function from a common ancestor. Proc. Natl. Acad. Sci. USA 71, 3888-3891
8. Hayashi, H., Mizuguchi, H., and Kagamiyama H. (1993) Rat liver aromatic L-aromatic acid decarboxylase: spectroscopic and kinetic analysis of the coenzyme and reaction intermediates. Biochemistry 32, 812-818
9. Hayashi, H., Tsukiyama F., Ishii S., Mizuguchi, H., and Kagamiyama H. (1999) Acid-basic 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 38, 15615-15622
10. Ishii, S., Mizuguchi, H., Nishino, J., Hayashi, H., and Kagamiyama, H. (1996) Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis. J. Biochem. 120, 369-376
11. Ishii, S., Hayashi, H., Okamoto, A., and Kagamiyama, H. (1998) Aromatic L-amino acid decarboxylase: conformational change in the flexible region around Arg334 is required during the transaldimination process. Protein Sci. 7, 1802-1810
12. Moore, P.S., Dominici, P., and Borri-Voltattorni, C. (1996) Cloning and expression of pig kidney dopa decarboxylase: comparison of the naturally occurring and recombinant enzymes. Biochem. J. 315, 249-256
13. Nishino, J., Hayashi, H., Ishii, S., and Kagamiyama, H. (1997) An anomalous side reaction of the Lys303 mutant aromatic L-amino acid decarboxylase unravels the role of the residue in catalysis. J. Biochem. 121, 604-611
14. Chu, W. and Metzler D.E. (1994) Enzymatically active truncated cat brain glutamate decarboxylase: expression, purification, and absorption spectrum. Arch. Biochem. Biophys. 313, 287-295
15. Osterman, A.L., Kinch, L.N., Grishin, N.V., and Phillips, M.A. (1995) Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis. J. Biol. Chem. 270, 11797-11802
16. Osterman, A.L., Brooks, H.B., Jackson, L., Abbott, J.J., and Phillips, M.A. (1999) Lysine-69 plays a key role in catalysis by ornithine decarboxylase through acceleration of the Schiff base formation, decarboxylation, and product release steps. Biochemistry 38, 11814-11826
17. Coleman, C.S., Stanley, B.A., Viswanath, R., and Pegg A.E. (1994) Rapid exchange of subunits of mammalian ornithine decarboxylase. J. Biol. Chem. 269, 3155-3158
18. Brooks, H.B. and Phillips, M.A. (1997) Characterization of the reaction mechanism for Trypanosoma brucei ornithine decarboxylase by multiwavelenghth stopped-flow spectroscopy. Biochemistry 36, 15147-15155
19. Tanase, S., Guirard, B.M., and Snell, E.E. (1985) Purification and properties of a pyridoxal 5′-phosphate-dependent histidine decarboxylase from Morganella morganii AM-15. J. Biol. Chem. 260, 6738-6746
20. Taguchi, Y., Watanabe, T., Kubota, H., Hayashi, H., and Wada, H. (1984) Purification of histidine decarboxylase from the liver of fetal rats and its immunochemical and immunohistochemical characterization. J. Biol. Chem. 259, 5214-5221
21. Engel, N., Olmo, M.T., Coleman, C.S., Medina M.A., Pegg, A.E., and Sánchez-Jiménez, F. (1996) Experimental evidence for structure/function features in common between mammalian histidine decarboxylase and ornithine decarboxylase. Biochem. J. 320, 365-368
22. Viguera, E., Trelles, O., Urdiales, J.L., Matés, J.M., and Sánchez-Jiménez, F. (1994) Mammalian L-amino acid decarboxylases producing 1,4-diamines: analogies among differences. Trends Biochem. Sci. 19, 318-319
23. Olmo, M.T., Urdiales, J.L., Pegg, A.E., Medina, M.A., and Sánchez-Jiménez, F. (2000) In vitro study of proteolytic degradation of rat histidine decarboxylase. Eur. J. Biochem. 267, 1527-1531
24. Ohmori, E., Fukui, T., Imanishi, N., Yatsunami, K., and Ichikawa, A. (1990) Purification and characterization of L-histidine decarboxylase from mouse mastocytoma P-815 cells. J. Biochem. 107, 834-839
25. Dartsch, C., Chen, D., Hakanson, R., and Persson, L. (1999) Multiple forms of rat stomach histidine decarboxylase may reflect post-translational activation of the enzyme. Regul. Peptides 81, 41-48
26. Fleming, J.W. and Wang, T.C. (2000) Amino and carboxyterminal PEST domain mediate gastrin stabilization of rat L-histidine decarboxylase isoforms. Mol. Cell Biol. 20, 4932-4947
27. Fajardo, I., Urdiales, J.L., Medina, M.A., and Sánchez-Jiménez, F. (2001) Effects of phorbol ester and dexamethasone treatment on histidine decarboxylase and ornithine decarboxylase in basophilic cells. Biochem. Pharmacol. 61, 1101-1106
28. Kuramitsu, S., Hiromi, K., Hayashi, H., Morino, Y., and Kagamiyama, H. (1990) Pre-steady state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodinamic aspects of its substrate specificity. Biochemistry 29, 5469-5476
29. Yamamoto, J., Fukui, T., Suzuki, K., Tanaka, S., Yatsunami, K., and Ichikawa, A. (1993) Expression and characterization of recombinant mouse mastocytoma histidine decarboxylase. Biochim. Biophys. Acta 1216, 431-440
30. Johnson, G.F., Tu, J.I., Bartlett, M.L., and Graves, D.J. (1970) Physical-chemical studies on the pyridoxal phosphate binding site in sodium borohydride-reduced and native phosphorylase. J. Biol. Chem. 245, 5560-5568
31. Honikel, K.O. and Madsen, N.B. (1972) Comparison of the absorbance spectra and fluorescence behavior of phosphorylase b with that of model pyridoxal phosphate derivatives in various solvents. J. Biol. Chem. 247, 1057-1064
32. Vazquez Segura, M.A., Donoso, J., Munoz, F., Blanco, F.G., Garcïa del Vado, M.A., and Echevarria, G. (1994) Photophysical study of the Schiff bases of 5′-deoxypyridoxal and n-hexylamine in cationic micelles. Photochem. Photobiol. 60, 399-404
33. Zhou, X., and Toney, M.D. (1999) pH studies on the mechanism of the pyridoxal phosphate-dependent dialkylglycine decarboxylase. Biochemistry 38, 311-320
34. Kallen, R.G., Korpela, T., Martell, A.E., Matsushima, Y., Metzler, C.M., Metzler, D.E., Morozov, Y.V., Ralston, I.M., Savin, F.A., Torchinsky, Y.M., and Ueno, H. (1985) in Transaminases (Metzler, D.E. and Christen, P., eds) pp. 37-108, John Wiley & Sons, New York
35. Hayashi, H. (1995) Pyridoxal enzymes: mechanistic diversity and uniformity. J. Biochem. 118, 463-473
36. a during catalysis. Biochemistry 37, 15076-15085