Crystal structure of cystalysin from Treponema denticola: a pyridoxal 5′‐phosphate‐dependent protein acting as a haemolytic enzyme
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[1] W. Blankenfeldt,et al. Crystal structure of trypanosoma cruzi tyrosine aminotransferase: Substrate specificity is influenced by cofactor binding mode , 2008, Protein science : a publication of the Protein Society.
[2] C. Walsh,et al. The behavior and significance of slow-binding enzyme inhibitors. , 2006, Advances in enzymology and related areas of molecular biology.
[3] G. Bourenkov,et al. X‐ray structure of MalY from Escherichia coli: a pyridoxal 5′‐phosphate‐dependent enzyme acting as a modulator in mal gene expression , 2000, EMBO Journal.
[4] G. Schneider,et al. Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes. , 1999, Journal of molecular biology.
[5] G. Kurzban,et al. Sulfhemoglobin formation in human erythrocytes by cystalysin, an L-cysteine desulfhydrase from Treponema denticola. , 1999, Oral microbiology and immunology.
[6] I. Miyahara,et al. Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate. , 1999, Biochemistry.
[7] J. Jansonius,et al. Structure, evolution and action of vitamin B6-dependent enzymes. , 1998, Current opinion in structural biology.
[8] R. Baxter,et al. The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. , 1998, Journal of molecular biology.
[9] R J Read,et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. , 1998, Acta crystallographica. Section D, Biological crystallography.
[10] H. Hayashi,et al. Transient-state kinetics of the reaction of aspartate aminotransferase with aspartate at low pH reveals dual routes in the enzyme-substrate association process. , 1997, Biochemistry.
[11] R. Huber,et al. Slow-binding inhibition of Escherichia coli cystathionine beta-lyase by L-aminoethoxyvinylglycine: a kinetic and X-ray study. , 1997, Biochemistry.
[12] G. Kurzban,et al. Cystalysin, a 46-kilodalton cysteine desulfhydrase from Treponema denticola, with hemolytic and hemoxidative activities , 1997, Infection and immunity.
[13] D. Metzler,et al. Refinement and Comparisons of the Crystal Structures of Pig Cytosolic Aspartate Aminotransferase and Its Complex with 2-Methylaspartate* , 1997, The Journal of Biological Chemistry.
[14] I. Leibrecht,et al. A Novel l-Cysteine/Cystine C-S-Lyase Directing [2Fe-2S] Cluster Formation of SynechocystisFerredoxin* , 1997, The Journal of Biological Chemistry.
[15] J. Gouaux,et al. Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore , 1996, Science.
[16] R. Huber,et al. Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A. , 1996, Journal of molecular biology.
[17] G. Kleywegt. Use of non-crystallographic symmetry in protein structure refinement. , 1996, Acta crystallographica. Section D, Biological crystallography.
[18] W. Huestis,et al. Hemoglobin oxidation products extract phospholipids from the membrane of human erythrocytes. , 1996, Biochemistry.
[19] S. Jones,et al. Principles of protein-protein interactions. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[20] P. Argos,et al. Knowledge‐based protein secondary structure assignment , 1995, Proteins.
[21] S. Holt,et al. The 46-kilodalton-hemolysin gene from Treponema denticola encodes a novel hemolysin homologous to aminotransferases , 1995, Infection and immunity.
[22] W. Boos,et al. MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase) , 1995, Journal of bacteriology.
[23] Collaborative Computational,et al. The CCP4 suite: programs for protein crystallography. , 1994, Acta crystallographica. Section D, Biological crystallography.
[24] J. Navaza,et al. AMoRe: an automated package for molecular replacement , 1994 .
[25] S. Holt,et al. Purification and characterization of a 45 kDa hemolysin from Treponema denticola ATCC 35404. , 1994, Microbial pathogenesis.
[26] S. Holt,et al. Characterization of hemolysis and hemoxidation activities by Treponema denticola. , 1994, Microbial pathogenesis.
[27] C. Sander,et al. Protein structure comparison by alignment of distance matrices. , 1993, Journal of molecular biology.
[28] P. Christen,et al. Aminotransferases: demonstration of homology and division into evolutionary subgroups. , 1993, European journal of biochemistry.
[29] J. Thompson,et al. Toxicity of Bordetella avium beta-cystathionase toward MC3T3-E1 osteogenic cells. , 1993, The Journal of biological chemistry.
[30] J. Thornton,et al. PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .
[31] V. Rastogi,et al. Cloning and nucleotide sequencing of Rhizobium meliloti aminotransferase genes: an aspartate aminotransferase required for symbiotic nitrogen fixation is atypical , 1993, Journal of bacteriology.
[32] H. Kagamiyama,et al. Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate. , 1992, Biochemistry.
[33] R. Huber,et al. Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement , 1991 .
[34] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[35] A. Okamoto,et al. Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization. , 1991, The Journal of biological chemistry.
[36] P. Delepelaire,et al. Protein secretion in gram-negative bacteria. The extracellular metalloprotease B from Erwinia chrysanthemi contains a C-terminal secretion signal analogous to that of Escherichia coli alpha-hemolysin. , 1990, The Journal of biological chemistry.
[37] M. B. Edlund,et al. The formation of hydrogen sulfide and methyl mercaptan by oral bacteria. , 1990, Oral microbiology and immunology.
[38] Portland Press Ltd. Sulphane sulphur in biological systems: a possible regulatory role , 1990 .
[39] J. Toohey. Sulphane sulphur in biological systems: a possible regulatory role. , 1989, The Biochemical journal.
[40] P. Christen,et al. Evolutionary relationships among aminotransferases , 1989 .
[41] W. Valentine,et al. Modification of erythrocyte enzyme activities by persulfides and methanethiol: possible regulatory role. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[42] K. J. Lee,et al. Membrane bilayer balance and erythrocyte shape: a quantitative assessment. , 1985, Biochemistry.
[43] J. Tonzetich,et al. Effect of Hydrogen Sulfide and Methyl Mercaptan on the Permeability of Oral Mucosa , 1984, Journal of dental research.
[44] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[45] C. Dwivedi,et al. Cloning, purification, and characterization of beta-cystathionase from Escherichia coli. , 1982, Biochemistry.
[46] J. Berger,et al. Antimetabolites produced by microorganisms. X. L-2-amino-4-(2-aminoethoxy)-trans-3-butenoic acid. , 1974, The Journal of antibiotics.
[47] A. Stempel,et al. ANTIMETABOLITES PRODUCED BY MICROORGANISMS. II , 1971 .
[48] J. L. Hilton,et al. Rhizobium-synthesized phytotoxin: An inhibitor of β-cystathionase in Salmonella typhimurium , 1968 .
[49] V. Luzzati,et al. Traitement statistique des erreurs dans la determination des structures cristallines , 1952 .
[50] Z. Otwinowski,et al. [20] Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[51] I. Holland,et al. Protein Secretion in Gram-Negative Bacteria , 1997 .
[52] A. Okamoto,et al. An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. , 1996, Journal of biochemistry.
[53] D. Oliver. Protein secretion in Escherichia coli. , 1985, Annual review of microbiology.
[54] J. Popp,et al. A critical review of the literature on hydrogen sulfide toxicity. , 1984, Critical reviews in toxicology.
[55] G. N. Ramachandran,et al. Conformation of polypeptides and proteins. , 1968, Advances in protein chemistry.