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Abstract:

Epimastigotes of Trypanosoma cruzi, the causative agent of Chagas disease, catabolize proteins and amino acids with production of NH3, and glucose with production of reduced catabolites, chiefly succinate and l-alanine, even under aerobic conditions. This "aerobic fermentation of glucose" is probably due to both the presence of low levels of some cytochromes, causing a relative inefficiency of the respiratory chain for NADH reoxidation during active glucose catabolism, and the lack of NADH dehydrogenase and phosphorylation site I, resulting in the entry of reduction equivalents into the chain mostly as succinate. Phosphoenol pyruvate carboxykinase and pyruvate kinase may play an essential role in diverting glucose carbon to succinate or l-alanine, and l-malate seems to be the major metabolite for the transport of glucose carbon and reduction equivalents between glycosome and mitochondrion. The parasite contains proteinase and peptidase activities. The major lysosomal cysteine proteinase, cruzipain, has been characterized in considerable detail, and might be involved in the host/parasite relationship, in addition to its obvious role in parasite nutrition. Among the enzymes of amino acid catabolism, two glutamate dehydrogenases (one NADP- and the other NAD-linked), alanine aminotransferase, and the major enzymes of aromatic amino acid catabolism (tyrosine aminotransferase and aromatic α-hydroxy acid dehydrogenase), have been characterized and proposed to be involved in the reoxidation of glycolytic NADH. © 1994 Plenum Publishing Corporation.

Registro:

Documento: Artículo
Título:Intermediate metabolism in Trypanosoma cruzi
Autor:Cazzulo, J.J.
Filiación:Instituto de Investigaciones Bioquímicas 'Luis F. Leloir.' Fundación Campomar, CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, A. Machado 151, Buenos Aires, 1405, Argentina
Palabras clave:aerobic fermentation of glucose; aromatic amino acid catabolism; cruzipain; glutamate dehydrogenases; transaminases; Trypanosoma cruzi; alanine; alanine aminotransferase; aromatic amino acid; cruzipain; glutamate dehydrogenase; malic acid; phosphoenolpyruvate carboxykinase (gtp); pyruvate kinase; succinic acid; tyrosine aminotransferase; amino acid metabolism; amino acid transport; bacterial metabolism; carbohydrate transport; glucose metabolism; nonhuman; protein degradation; protein metabolism; protein transport; respiratory chain; review; trypanosoma cruzi; Aerobiosis; Amino Acids; Ammonia; Animal; Biological Transport, Active; Carbohydrates; Fermentation; Glucose; Oxidation-Reduction; Protozoan Proteins; Support, Non-U.S. Gov't; Trypanosoma cruzi
Año:1994
Volumen:26
Número:2
Página de inicio:157
Página de fin:165
DOI: http://dx.doi.org/10.1007/BF00763064
Título revista:Journal of Bioenergetics and Biomembranes
Título revista abreviado:J Bioenerg Biomembr
ISSN:0145479X
CODEN:JBBID
CAS:alanine aminotransferase, 9000-86-6, 9014-30-6; alanine, 56-41-7, 6898-94-8; glutamate dehydrogenase, 9001-46-1; malic acid, 149-61-1, 6915-15-7; phosphoenolpyruvate carboxykinase (GTP), 9013-08-5; pyruvate kinase, 9001-59-6; succinic acid, 110-15-6; tyrosine aminotransferase, 9014-55-5; Amino Acids; Ammonia, 7664-41-7; Carbohydrates; Glucose, 50-99-7; Protozoan Proteins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0145479X_v26_n2_p157_Cazzulo

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Citas:

---------- APA ----------
(1994) . Intermediate metabolism in Trypanosoma cruzi. Journal of Bioenergetics and Biomembranes, 26(2), 157-165.
http://dx.doi.org/10.1007/BF00763064
---------- CHICAGO ----------
Cazzulo, J.J. "Intermediate metabolism in Trypanosoma cruzi" . Journal of Bioenergetics and Biomembranes 26, no. 2 (1994) : 157-165.
http://dx.doi.org/10.1007/BF00763064
---------- MLA ----------
Cazzulo, J.J. "Intermediate metabolism in Trypanosoma cruzi" . Journal of Bioenergetics and Biomembranes, vol. 26, no. 2, 1994, pp. 157-165.
http://dx.doi.org/10.1007/BF00763064
---------- VANCOUVER ----------
Cazzulo, J.J. Intermediate metabolism in Trypanosoma cruzi. J Bioenerg Biomembr. 1994;26(2):157-165.
http://dx.doi.org/10.1007/BF00763064