Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: stereochemical implications of PLP-dependent amino acid decarboxylases

Structure - Tập 7 Số 5 - Trang 567-581 - 1999
Andrew D. Kern1, Marcos Antônio de Oliveira1, Philip Coffino2, Marvin L. Hackert3,4
1Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA
2Department of Microbiology and Immunology, School of Medicine, University of California at San Francisco, San Francisco, CA 94143, USA
3Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, TX 78712, USA E-mail:
4[email protected]

Tóm tắt

Từ khóa


Tài liệu tham khảo

Martell, 1982, Reaction pathways and mechanisms of pyridoxal catalysis, Adv. Enzymol. Relat. Areas Mol. Biol, 53, 163

Jansonius, 1998, Structure, evolution and action of vitamin B6-dependent enzymes, Curr. Opin. Struct. Biol, 8, 759, 10.1016/S0959-440X(98)80096-1

Ford, 1980, Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase, Proc. Natl Acad. Sci. USA, 77, 2559, 10.1073/pnas.77.5.2559

Hyde, 1988, Three-dimensional structure of the tryptophan synthase α2β2 multienzyme complex from Salmonella typhimurium, J. Biol. Chem, 263, 17857, 10.1016/S0021-9258(19)77913-7

Shaw, 1997, Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9 Å resolution, Biochemistry, 36, 1329, 10.1021/bi961856c

Sugio, 1995, Crystal structure of a D-amino acid aminotransferase: How the protein controls stereoselectivity, Biochemistry, 34, 9661, 10.1021/bi00030a002

Gallagher, 1998, Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase, Structure, 6, 465, 10.1016/S0969-2126(98)00048-3

Isupov, 1998, Crystal structure of tryptophanase, J. Mol. Biol, 276, 603, 10.1006/jmbi.1997.1561

Shen, 1998, Crystal structure of human recombinant ornithine aminotransferase, J. Mol. Biol, 277, 81, 10.1006/jmbi.1997.1583

Hennig, 1997, Crystal structure of glutamate-1-semialdehyde aminomutase: an α2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity, Proc. Natl Acad. Sci. USA, 94, 4866, 10.1073/pnas.94.10.4866

Clausen, 1996, Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83 Å, J. Mol. Biol, 262, 202, 10.1006/jmbi.1996.0508

Toney, 1993, Dialkylglycine decarboxylase structure: Bifunctional active site and alkali metal sites, Science, 261, 756, 10.1126/science.8342040

Antson, 1993, Three-dimensional structure of tyrosine phenollyase, Biochemistry, 32, 4195, 10.1021/bi00067a006

Momany, 1995, Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 Å resolution, J. Mol. Biol, 252, 643, 10.1006/jmbi.1995.0526

Dunathan, 1966, Conformation and reaction specificity in pyridoxal phosphate enzymes, Proc. Natl Acad. Sci. USA, 55, 712, 10.1073/pnas.55.4.712

Tabor, 1984, Polyamines, Annu. Rev. Biochem, 53, 749, 10.1146/annurev.bi.53.070184.003533

Luk, 1982, Ornithine decarboxylase: essential in proliferation but not differentiation of human promyelocytic leukemia cells, Science, 216, 75, 10.1126/science.6950518

Cohen, 1970, Estrogenic induction of ornithine decarboxylase in vivo and in vitro, Science, 170, 336, 10.1126/science.170.3955.336

Russel, 1968, Amine synthesis in rapidly growing tissues: ornithine decarboxylase activity in regenerating rat liver, chick embryo, and various tumors, Proc. Natl Acad. Sci. USA, 60, 1420, 10.1073/pnas.60.4.1420

Poulin, 1995, Induction of apoptosis by excessive polyamine accumulation in ornithine decarboxylase-overproducing L1210 cells, Biochem. J, 311, 723, 10.1042/bj3110723

Pegg, 1988, Polyamine metabolism and its importance in neoplastic growth and as a target for chemotherapy, Cancer Res, 48, 759

Auvinen, 1992, Ornithine decarboxylase activity is critical for cell transformation, Nature, 360, 355, 10.1038/360355a0

Pegg, 1995, Ornithine decarboxylase as a target for chemoprevention, J. Cell Biochem. Suppl, 22, 132, 10.1002/jcb.240590817

Bacchi, 1994, Combination chemotherapy of drug-resistant Trypanosoma brucei rhodesiense infections in mice using DL-α-difluoromethylornithine and standard trypanocides, Antimicrob. Agents Chemother, 38, 563, 10.1128/AAC.38.3.563

Meyskens, 1995, Development of difluoromethylorntihine as a chemoprevention agent for the management of colon cancer, J. Cell Biochem. Suppl, 22, 126, 10.1002/jcb.240590816

Mitchell, 1998, Phase I dose deescalation trial of α-difluoromethylornithine in patients with grade 3 cervical intraepithelial neoplasia, Clin. Cancer Res, 4, 303

Sandmeier, 1994, Multiple evolutionary origin of pyridoxal-5′-phosphate-dependent amino acid decarboxylases, Eur. J. Biochem, 221, 997, 10.1111/j.1432-1033.1994.tb18816.x

Momany, 1995, Structural motifs for pyridoxal-5′-phosphate binding in decarboxylases: an analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase, Prot. Sci, 4, 849, 10.1002/pro.5560040504

Grishin, 1995, Modeling of the spatial structure of eukaryotic ornithine decarboxylase, Prot. Sci, 4, 1291, 10.1002/pro.5560040705

Abrahamsen, 1992, Multiple elements responsible for transcriptional regulation of the ornithine decarboxylase gene by protein kinase A, J. Biol. Chem, 267, 18866, 10.1016/S0021-9258(19)37041-3

Reddy, 1996, Multisite phosphorylation of ornithine decarboxylase in transformed macrophages results in increased intracellular enzyme stability and catalytic efficiency, J. Biol. Chem, 271, 24945, 10.1074/jbc.271.40.24945

Rosenberg-Hasson, 1991, Mouse ornithine decarboxylase is phosphorylated by casein kinase-II at a predominant single location (serine 303), Eur. J. Biochem, 197, 419, 10.1111/j.1432-1033.1991.tb15927.x

Hayashi, 1996, Ornithine decarboxylase antizyme: a novel type of regulatory protein, Trends Biochem. Sci, 21, 27, 10.1016/S0968-0004(06)80024-1

Heller, 1976, Induction of a protein inhibitor to ornithine decarboxylase by the end product of its reaction, Proc. Natl Acad. Sci. USA, 73, 1858, 10.1073/pnas.73.6.1858

Mitchell, 1990, Conformational changes in ornithine decarboxylase enable recognition by antizyme, Biochim. Biophys. Acta, 1037, 115, 10.1016/0167-4838(90)90109-S

Murakami, 1992, Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination, Nature, 360, 597, 10.1038/360597a0

Murakami, 1996, Cloning of antizyme inhibitor, a highly homologous protein to ornithine decarboxylase, J. Biol. Chem, 271, 3340, 10.1074/jbc.271.7.3340

Fujita, 1982, A macromolecular inhibitor of the antizyme to ornithine decarboxylase, Biochem. J, 204, 647, 10.1042/bj2040647

Kern, 1996, Crystallization of a mammalian ornithine decarboxylase, Proteins, 24, 266, 10.1002/(SICI)1097-0134(199602)24:2<266::AID-PROT15>3.0.CO;2-L

Ghoda, 1989, Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation, Science, 243, 1493, 10.1126/science.2928784

Banner, 1975, Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 Å resolution using amino acid sequence data, Nature, 255, 609, 10.1038/255609a0

Osterman, 1995, Domain organization and a protease-sensitive loop in eukaryotic ornithine decarboxylase, Biochemistry, 34, 13431, 10.1021/bi00041a021

Coleman, 1994, Rapid exchange of subunits of mammalian ornithine decarboxylase, J. Biol. Chem, 269, 3155, 10.1016/S0021-9258(17)41842-4

Tobias, 1993, Gly387 of murine ornithine decarboxylase is essential for the formation of stable homodimers, Eur. J. Biochem, 218, 245, 10.1111/j.1432-1033.1993.tb18371.x

Tobias, 1993, Intersubunit location of the active site of mammalian ornithine decarboxylase as determined by hybridization of site-directed mutants, Biochemistry, 32, 5842, 10.1021/bi00073a017

Osterman, 1994, Formation of functional cross-species heterodimers of ornithine decarboxylase, Biochemistry, 33, 13662, 10.1021/bi00250a016

Jones, 1996, Principles of protein–protein interactions, Proc. Natl Acad. Sci. USA, 93, 13, 10.1073/pnas.93.1.13

Li, 1992, Regulated degradation of ornithine decarboxylase requires interaction with the polyamine-inducible protein antizyme, Mol. Cell Biol, 12, 3556, 10.1128/MCB.12.8.3556

Li, 1993, Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein, Mol. Cell. Biol, 13, 2377, 10.1128/MCB.13.4.2377

Tsirka, 1992, Dominant negative mutants of ornithine decarboxylase, J. Biol. Chem, 267, 23057, 10.1016/S0021-9258(18)50055-7

Osterman, 1997, Role of Arg-277 in the binding of pyridoxal-5′-phosphate to Trypanosoma brucei ornithine decarboxylase, Biochemistry, 36, 4558, 10.1021/bi962916h

Osterman, 1995, Acidic residues important for substrate binding and cofactor reactivity in eukaryotic ornithine decarboxylase identified by alanine scanning mutagenesis, J. Biol. Chem, 270, 11797, 10.1074/jbc.270.20.11797

Yano, 1993, A hydrogen-bonding network modulating enzyme function: asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase, Biochemistry, 32, 1810, 10.1021/bi00058a015

Brooks, 1997, Characterization of the reaction mechanism for Trypanosoma brucei ornithine decarboxylase by multiwavelength stopped-flow spectroscopy, Biochemistry, 36, 15147, 10.1021/bi971652b

Stamper, 1998, Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine, Biochemistry, 37, 10438, 10.1021/bi980692s

Kirsch, 1984, Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure, J. Mol. Biol, 174, 497, 10.1016/0022-2836(84)90333-4

Tobler, 1987, Stereospecific labilization of the C-4′ pro-S hydrogen of pyridoxamine 5′-phosphate in aspartate aminotransferase, J. Biol. Chem, 262, 8985, 10.1016/S0021-9258(18)48034-9

Metzler, 1988, Correlation of polarized absorption spectroscopic and X-ray diffraction studies of crystalline cytosolic aspartate aminotransferase of pig hearts, J. Mol. Biol, 203, 197, 10.1016/0022-2836(88)90102-7

Julin, 1989, Kinetic isotope effect studies on aspartate aminotransferase: evidence for a concerted 1,3 prototropic shift mechanism for the cytoplasmic isozyme and L-aspartate and dichotomy in mechanism, Biochemistry, 28, 3825, 10.1021/bi00435a031

Toney, 1993, Lysine 258 in aspartate aminotransferase: enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift, Biochemistry, 32, 1471, 10.1021/bi00057a010

Malashkevich, 1993, Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase, Biochemistry, 32, 13451, 10.1021/bi00212a010

Hayashi, 1998, The imine-pyridine torsion of the pyridoxal 5′-phosphate Schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis, Biochemistry, 37, 15076, 10.1021/bi981517e

Gani, 1991, Structural and mechanistic comparison of pyridoxal-5′-phosphate dependent decarboxylase and transaminase enzymes, Philos. Trans. R. Soc. Lond. B. Biol. Sci, 332, 131, 10.1098/rstb.1991.0041

Coleman, 1993, Effect of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site-directed irreversible inhibitors, J. Biol. Chem, 268, 24572, 10.1016/S0021-9258(19)74505-0

Asada, 1981, Stereochemistry of meso-α,ϵ-diaminopimelate decarboxylase reaction: the first evidence for pyridoxal-5′-phosphate dependent decarboxylation with inversion of configuration, Biochemistry, 20, 6881, 10.1021/bi00527a022

Asada, 1984, Stereochemistry of ornithine decarboxylase reaction, J. Biochem, 95, 277, 10.1093/oxfordjournals.jbchem.a134594

Lim, 1998, Nonstereospecific transamination catalyzed by pyridoxal phosphate-dependent amino acid racemases of broad substrate specificity, J. Biol. Chem, 273, 4001, 10.1074/jbc.273.7.4001

Coffino, 1998, Degradation of Ornithine Decarboxylase, 411

Thiel, 1995, Macromolecular crystallographic results obtained at CHESS using a detector incorporating a charge-coupled device, Rev. Sci. Instrum, 66, 1477, 10.1063/1.1145946

Otwinowski, 1997, Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol, 276, 307, 10.1016/S0076-6879(97)76066-X

Otwinowski, 1991, Maximum likelihood refinement of heavy atom parameters, 80

Perrakis, 1997, wARP: Improvement and extension of crystallographic phases by weighted averaging of multiple-refined dummy atomic models, Acta Crystallogr. D, 53, 448, 10.1107/S0907444997005696

Jones, 1991, Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A, 47, 110, 10.1107/S0108767390010224

Brünger, 1992

Murshudov, 1997, Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr.D, 53, 240, 10.1107/S0907444996012255

Laskowski, 1993, PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr, 26, 283, 10.1107/S0021889892009944

Hooft, 1996, Errors in protein structures, Nature, 381, 272, 10.1038/381272a0

Kleywegt, 1997, Validation of protein models from Cα coordinates alone, J. Mol. Biol, 273, 371, 10.1006/jmbi.1997.1309

1994, The CCP4 suite Programs for Protein Crystallography, Acta Crystallogr.D, 50, 760, 10.1107/S0907444994003112

Kraulis, 1991, MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr, 24, 946, 10.1107/S0021889891004399

Merrit, 1994, Raster3D Version 2.0. A program for photorealistic molecular graphics, Acta Crystallogr. D, 50, 869, 10.1107/S0907444994006396

Nicholls, 1991, Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons, Proteins, 11, 281, 10.1002/prot.340110407

Esnouf, 1997, An extensively modified version of MolScript that includes greatly enhanced coloring capabilities, J. Mol. Graph. Model, 15, 112, 10.1016/S1093-3263(97)00021-1