| Full text | |
| Author(s): |
Sculaccio, S. A.
[1, 2, 3]
;
Rodrigues, E. M.
[2]
;
Cordeiro, A. T.
[2]
;
Magalhaes, A.
[2]
;
Braga, A. L.
[4]
;
Alberto, E. E.
[4]
;
Thiemann, O. H.
[1, 2, 3]
Total Authors: 7
|
| Affiliation: | [1] Univ Fed Sao Carlos, Dept Genet & Evolut, BR-13560 Sao Carlos, SP - Brazil
[2] Univ Sao Paulo, Inst Phys, BR-13566590 Sao Carlos, SP - Brazil
[3] Inst Chem, Chromatog Grp, Sao Carlos, SP - Brazil
[4] Univ Fed Santa Maria, Dept Chem, BR-97105900 Santa Maria, RS - Brazil
Total Affiliations: 4
|
| Document type: | Journal article |
| Source: | Molecular and Biochemical Parasitology; v. 162, n. 2, p. 165-171, DEC 2008. |
| Web of Science Citations: | 20 |
| Abstract | |
Selenophosphate synthetase (EC 2.7.9.3), the product of the selD gene, produces the biologically selenium donor compound, monoselenophosphate, from ATP and selenide, for the synthesis of cysteine. The kinetoplastid Leishmania major and Trypanosoma brucei selD genes were cloned and the protein overexpressed and purified to apparent homogeneity. The selD gene in L. major and T brucei respectively 1197 and 1179 bp long encoding proteins of 399 and 393 amino acids with molecular of 42.7 and 43 kDa. The molecular mass of 100 kDa for both (L. major and T brucei) SEWS is consistent dimeric proteins. The kinetoplastid selD complement Escherichia call (WL400) selD deletion it is a functional enzyme and the specific activity of these enzymes was determined. A conserved residue was identified both by multiple sequence alignment as well as by functional and activity assay of the mutant (Cys to Ala) forms of the SELD identifying this residue as essential for catalytic function. (C) 2008 Elsevier B.V. All rights reserved. (AU) | |