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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Biochemical characterization of serine acetyltransferase and cysteine desulfhydrase from Leishmania major

Texto completo
Marciano, Daniela [1] ; Santana, Marianela [1] ; Mantilla, Brian Suarez [2] ; Silber, Ariel Mariano [2] ; Marino-Buslje, Cristina [1, 2] ; Nowicki, Cristina [1]
Número total de Autores: 6
Afiliação do(s) autor(es):
[1] Univ Buenos Aires, Inst Quim & Fisicoquim Biol, IQUIFIB CONICET, Fac Farm & Bioquim, Buenos Aires, DF - Argentina
[2] Univ Sao Paulo, Inst Ciencias Biomed, Dept Parasitol, BR-05508 Sao Paulo - Brazil
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: Molecular and Biochemical Parasitology; v. 173, n. 2, p. 170-174, OCT 2010.
Citações Web of Science: 6

Cysteine metabolism exhibits atypical features in Leishmania parasites. The nucleotide sequence annotated as LmjF32.2640 encodes a cysteine desulfhydrase, which specifically catalyzes the breakdown of cysteine into pyruvate, NH(3) and H(2)S. Like in other pathogens, this capacity might be associated with regulatory mechanisms to control the intracellular level of cysteine, a highly toxic albeit essential amino acid, in addition to generate pyruvate for energy production. Besides, our results provide the first insight into the biochemical properties of Leishmania major serine acetyltransferase (SAT), which is likely involved in the two routes for de novo synthesis of cysteine in this pathogen. When compared with other members of SAT family, the N-terminal region of L. major homologue is uniquely extended, and seems to be essential for proper protein folding. Furthermore, unlike plant and bacterial enzymes, the carboxy-terminal-C(10) sequence stretch of L major SAT appears not to be implicated in forming a tight bi-enzyme complex with cysteine synthase. (C) 2010 Elsevier B.V. All rights reserved. (AU)

Processo FAPESP: 08/57596-4 - Metabolismo de aminoácidos de Trypanosoma cruzi: alvos putativos para terapia
Beneficiário:Ariel Mariano Silber
Linha de fomento: Auxílio à Pesquisa - Regular