Purification and partial structural and kinetic characterization of an aromatic L-α-hydroxy acid dehydrogenase from epimastigotes of Trypanosoma cruzi
An aromatic L-α-hydroxyacid dehydrogenase (AHADH) was purified to homogeneity from epimastigotes of Trypanosoma cruzi by a method involving chromatography on DEAE-cellulose, hydrophobic interaction chromatography on Phenyl-Sepharose and affinity chromatography on Affi-Gel Blue. The purified enzyme s...
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1994
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| LEADER | 10174caa a22010937a 4500 | ||
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| 001 | PAPER-55 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518202926.0 | ||
| 008 | 190411s1994 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0028079911 | |
| 024 | 7 | |2 cas |a Alcohol Oxidoreductases, EC 1.1; Amino Acids; D-2-hydroxyacid dehydrogenase, EC 1.1.99.6; D-lactate dehydrogenase, EC 1.1.1.28 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a MBIPD | ||
| 100 | 1 | |a Montemartini, M. | |
| 245 | 1 | 0 | |a Purification and partial structural and kinetic characterization of an aromatic L-α-hydroxy acid dehydrogenase from epimastigotes of Trypanosoma cruzi |
| 260 | |c 1994 | ||
| 270 | 1 | 0 | |m Montemartini, M.; IQUIFIB (UBA-CONICET), Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junin 956, 1113 Buenos Aires, Argentina |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Stibbs, Seed, Metabolism of tyrosine and phenylalanine in Trypanosoma brucei gambiense (1975) Int. J. Biochem., 6, pp. 197-203 | ||
| 504 | |a Stibbs, Seed, Further studies on the metabolism of tryptophan in Trypanosoma brucei gambiense: cofactors, inhibitors, and end-products (1975) Experientia, 31, pp. 274-277 | ||
| 504 | |a Stibbs, Seed, Short-term metabolism of (14C)tryptophan in rats infected with Trypanosoma brucei gambiense (1975) J. Infect. Dis., 131, pp. 459-462 | ||
| 504 | |a Constantsas, Levis, Vakirtzi-Lemonias, Crithidia fasciculata tyrosine aminotransferase (1971) I. Development, characterization and differentiation from alanine aminotransferase, 230, pp. 137-145. , 2nd Edn., Biochim. Biophys. Acta | ||
| 504 | |a Rege, Purification and characterization of a tyrosine aminotransferase from Crithidia fasciculata (1987) Mol. Biochem. Parasitol., 25, pp. 1-9 | ||
| 504 | |a Chatterjee, Ghosh, Transaminases of Leishmania donovani, the causative organism of Kala-azar (1957) Nature, 180, p. 1425 | ||
| 504 | |a Leelayoova, Marbury, Rainey, Mackenzie, Hall, In vitro tryptophan catabolism by Leishmania donovani donovani promastigotes (1992) J. Protozool., 39, pp. 350-358 | ||
| 504 | |a Nowicki, Montemartini, Duschak, Santomé, Cazzulo, Presence and subcellular localization of tyrosine aminotransferase and p-hydroxyphenyl lactate dehydrogenase in epimastigotes of Trypanosoma cruzi (1992) FEMS Microbiol. Lett., 92, pp. 119-124 | ||
| 504 | |a Montemartini, Santomé, Cazzulo, Nowicki, Purification and partial structural and kinetic characterization of tyrosine aminotransferase from epimastigotes of Trypanosoma cruzi (1993) Biochem. J., 292, pp. 901-906 | ||
| 504 | |a Jean, De Moss, Indolelactate dehydrogenase fromClostridium sporogenes (1968) Canadian Journal of Microbiology, 14, pp. 429-435 | ||
| 504 | |a Zannoni, Weber, Isolation and properties of aromatic α-keto acid reductase (1965) J. Biol. Chem., 241, pp. 1340-1344 | ||
| 504 | |a Bode, Lippoldt, Birnbaum, Purification and properties of D-aromatic lactate dehydrogenase (1986) An enzyme involved in the catabolism of the aromatic amino acids in Candida maltosa, 181, pp. 189-198. , 2nd Edn., Biochem. Physiol. Pflanzen | ||
| 504 | |a Coronel, Rovai, Gerez de Burgos, Burgos, Blanco, Properties of α-hydroxyacid dehydrogenase isozymes from Trypanosoma cruzi (1981) Mol. Biochem. Parasitol., 4, pp. 29-38 | ||
| 504 | |a Cazzulo, The aerobic fermentation of glucose by Trypanosomatids (1992) FASEB J., 6, pp. 3153-3161 | ||
| 504 | |a Cazzulo, Franke de Cazzulo, Engel, Cannata, End products and enzyme levels of aerobic glucose fermentation in Trypanosomatids (1985) Mol. Biochem. Parasitol., 16, pp. 329-343 | ||
| 504 | |a Fraser, Suzuki, The use of least squares in the data analysis (1973) Physical Principles and Techniques of Protein Chemistry, 21, pp. 301-355. , 2nd Edn., S.J. Leach, Academic Press, New York, Part C | ||
| 504 | |a Bradford, A rapid quantitative method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254 | ||
| 504 | |a Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-695 | ||
| 504 | |a Oakley, Kirsch, Morris, A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels (1980) Anal. Biochem., 105, pp. 361-363 | ||
| 504 | |a Edelhoch, Spectroscopic determination of tryptophan and tyrosine in proteins (1967) Biochemistry, 6, pp. 1948-1954 | ||
| 504 | |a Charbonneau, Strategies for obtaining partial amino acid sequence data from small quantities (< 5 nmol) of pure and partially purified protein (1989) A practical guide to protein and peptide purification for microsequencing, pp. 15-30. , P.T. Matsudaira, Academic Press, San Diego, CA | ||
| 504 | |a Birktoft, Fernley, Bradshaw, Banaszak, Aminoacid and sequence homology among the 2-hydroxyacid dehydrogenases: mitochondrial and cytoplasmic malate dehydrogenases form a homologous system with lactate dehydrogenases (1982) Proc. Nat. Acad. Sci. USA, 79, pp. 6166-6170. , 2nd Edn | ||
| 504 | |a Birktoft, Banaszak, The presence of a histidine-aspartic acid pair in the active site of 2-hydroxyacid dehydrogenases (1983) J. Biol. Chem., 258, pp. 472-482 | ||
| 504 | |a Montemartini, Santomé, Cazzulo, Nowicki, Production of aromatic α-hydroxyacids by epimastigotes of Trypanosoma cruzi, and its possible role in NADH re-oxidation (1994) FEMS Microbiol. Lett., 118, pp. 89-92 | ||
| 504 | |a Joh, Takeshima, Tsusuki, Setoyama, Shimada, Tanase, Kuramitsu, Morino, Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenases (1987) J. Biol. Chem., 262, pp. 15127-15131 | ||
| 504 | |a Eventoff, Rossmann, Taylor, Torff, Meyer, Keil, Kiltz, Structural adaptation of lactic dehydrogenase isozymes (1977) Proc. Nat. Acad. Sci. USA, 74, pp. 2677-2681. , 2nd Edn | ||
| 504 | |a Barker, Dayhoff, Detecting distant relationships: Computer methods and results (1972) Atlas of Protein Sequence and Structure, 5, pp. 101-110. , 2nd Edn., M.O. Dayhoff, National Biomedical Research Foundation, Washington, DC | ||
| 520 | 3 | |a An aromatic L-α-hydroxyacid dehydrogenase (AHADH) was purified to homogeneity from epimastigotes of Trypanosoma cruzi by a method involving chromatography on DEAE-cellulose, hydrophobic interaction chromatography on Phenyl-Sepharose and affinity chromatography on Affi-Gel Blue. The purified enzyme showed a single band in SDS-PAGE, with an apparent molecular mass of 36 kDa. Since the apparent molecular mass of the native enzyme, determined by gel filtration, is about 80 kDa, the native enzyme is a dimer of similar subunits. The amino acid composition was determined, as well as the sequences of 4 internal peptides obtained by CNBr cleavage at Met residues, and one peptide obtained after tryptic digestion. Three of the peptides presented considerable sequence similarity with the corresponding sequences of several malate dehydrogenases. The optimal pH for the enzyme reaction with p-hydroxyphenyl pyruvate and NADH as substrates was 7.5; that for the reverse reaction was 9.5. The apparent Km values for phenylpyruvate and p-hydroxyphenylpyruvate were 48 and 117μM, respectively; that for l-phenyllactate in the reverse reaction was 420μM. The enzyme was much less active with α-isocaproic acid as substrate, and other acids, including pyruvic and oxaloacetic, were not substrates at all. l-phenyllactic acid, but not the d-isomer, acted as substrate. The enzyme can therefore be considered as a general aromatic l-α-hydroxyacid dehydrogenase. The low apparent Km value for NADH (25 μM in the presence of phenylpyruvate) makes AHADH a candidate for the reoxidation of cytosolic NADH in T. cruzi. © 1994. |l eng | |
| 593 | |a IQUIFIB (UBA-CONICET), Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Junin 956, 1113 Buenos Aires, Argentina | ||
| 593 | |a Instituto de Investigaciones Bioquímicas 'Luis F. Leloir', Fundación Campomar, CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, A. Machado 151, 1405 Buenos Aires Argentina | ||
| 690 | 1 | 0 | |a AMINO ACID CATABOLISM |
| 690 | 1 | 0 | |a AROMATIC AMINO ACID |
| 690 | 1 | 0 | |a AROMATIC HYDROXYACID |
| 690 | 1 | 0 | |a DEHYDROGENASE |
| 690 | 1 | 0 | |a EPIMASTIGOTE |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a OXIDOREDUCTASE |
| 690 | 1 | 0 | |a ANIMAL EXPERIMENT |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CONTROLLED STUDY |
| 690 | 1 | 0 | |a ENZYME ANALYSIS |
| 690 | 1 | 0 | |a ENZYME PURIFICATION |
| 690 | 1 | 0 | |a EPIMASTIGOTE |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN DEGRADATION |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a ALCOHOL OXIDOREDUCTASES |
| 690 | 1 | 0 | |a AMINO ACID SEQUENCE |
| 690 | 1 | 0 | |a AMINO ACIDS |
| 690 | 1 | 0 | |a ANIMAL |
| 690 | 1 | 0 | |a COMPARATIVE STUDY |
| 690 | 1 | 0 | |a HYDROGEN-ION CONCENTRATION |
| 690 | 1 | 0 | |a KINETICS |
| 690 | 1 | 0 | |a MOLECULAR SEQUENCE DATA |
| 690 | 1 | 0 | |a MOLECULAR STRUCTURE |
| 690 | 1 | 0 | |a MOLECULAR WEIGHT |
| 690 | 1 | 0 | |a SEQUENCE HOMOLOGY, AMINO ACID |
| 690 | 1 | 0 | |a SUBSTRATE SPECIFICITY |
| 690 | 1 | 0 | |a SUPPORT, NON-U.S. GOV'T |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 690 | 1 | 0 | |a ANIMALIA |
| 690 | 1 | 0 | |a TRYPANOSOMA |
| 690 | 1 | 0 | |a TRYPANOSOMA CRUZI |
| 700 | 1 | |a Santomé, JosA. | |
| 700 | 1 | |a Cazzulo, J.J. | |
| 700 | 1 | |a Nowicki, C. | |
| 773 | 0 | |d 1994 |g v. 68 |h pp. 15-23 |k n. 1 |p Mol. Biochem. Parasitol. |x 01666851 |w (AR-BaUEN)CENRE-6136 |t Molecular and Biochemical Parasitology | |
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| 856 | 4 | 0 | |u https://doi.org/10.1016/0166-6851(94)00145-6 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_01666851_v68_n1_p15_Montemartini |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_01666851_v68_n1_p15_Montemartini |y Registro en la Biblioteca Digital |
| 961 | |a paper_01666851_v68_n1_p15_Montemartini |b paper |c PE | ||
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| 963 | |a VARI | ||
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