Literature DB >> 6336744

Iron-containing superoxide dismutase from Crithidia fasciculata. Purification, characterization, and similarity to Leishmanial and trypanosomal enzymes.

N Le Trant, S R Meshnick, K Kitchener, J W Eaton, A Cerami.   

Abstract

Leishmania tropica, Trypanosoma brucei, Trypanosoma cruzi, and Crithidia fasciculata have superoxide dismutases which are insensitive to cyanide and sensitive to peroxide and azide, properties characteristic of iron-containing superoxide dismutase. Studies on the superoxide dismutase of C. fasciculata have revealed that: 1) the enzyme is located in the cytosol; 2) isozymes exist; 3) the major superoxide dismutase isozyme (superoxide dismutase 2) has Mr approximately equal to 43,000 and consists of two equal-sized subunits, each of which contains 1.4 atoms of iron. Comparisons of the amino acid content of this crithidial superoxide dismutase with those of superoxide dismutases from other sources suggests that the crithidial enzyme is closely related to bacterial Fe-containing superoxide dismutases, and only distantly related to human Mn- and Cu,Zn-containing superoxide dismutases and to Euglena Fe-containing superoxide dismutase. Attempts are now underway to develop specific inhibitors of the trypanosomatid superoxide dismutase which may be of use in the treatment of leishmaniasis or trypanosomiasis.

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Year:  1983        PMID: 6336744

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  14 in total

1.  Identification of a developmentally regulated iron superoxide dismutase of Trypanosoma brucei.

Authors:  M Kabiri; D Steverding
Journal:  Biochem J       Date:  2001-11-15       Impact factor: 3.857

2.  Characterization of a cDNA encoding a cysteine-rich cell surface protein located in the flagellar pocket of the protozoan Trypanosoma brucei.

Authors:  M G Lee; B E Bihain; D G Russell; R J Deckelbaum; L H Van der Ploeg
Journal:  Mol Cell Biol       Date:  1990-09       Impact factor: 4.272

3.  Characterization of iron superoxide dismutase cDNAs from plants obtained by genetic complementation in Escherichia coli.

Authors:  W Van Camp; C Bowler; R Villarroel; E W Tsang; M Van Montagu; D Inzé
Journal:  Proc Natl Acad Sci U S A       Date:  1990-12       Impact factor: 11.205

4.  Down-regulation of Leishmania donovani trypanothione reductase by heterologous expression of a trans-dominant mutant homologue: effect on parasite intracellular survival.

Authors:  J Tovar; M L Cunningham; A C Smith; S L Croft; A H Fairlamb
Journal:  Proc Natl Acad Sci U S A       Date:  1998-04-28       Impact factor: 11.205

Review 5.  Superoxide dismutases and superoxide reductases.

Authors:  Yuewei Sheng; Isabel A Abreu; Diane E Cabelli; Michael J Maroney; Anne-Frances Miller; Miguel Teixeira; Joan Selverstone Valentine
Journal:  Chem Rev       Date:  2014-04-01       Impact factor: 60.622

6.  Escherichia coli iron superoxide dismutase targeted to the mitochondria of yeast cells protects the cells against oxidative stress.

Authors:  R Balzan; W H Bannister; G J Hunter; J V Bannister
Journal:  Proc Natl Acad Sci U S A       Date:  1995-05-09       Impact factor: 11.205

7.  Molecular cloning, characterization, and expression in Escherichia coli of iron superoxide dismutase cDNA from Leishmania donovani chagasi.

Authors:  S O Ismail; Y A Skeiky; A Bhatia; L A Omara-Opyene; L Gedamu
Journal:  Infect Immun       Date:  1994-02       Impact factor: 3.441

8.  Leishmanial glycosomes contain superoxide dismutase.

Authors:  R Dey; S C Datta
Journal:  Biochem J       Date:  1994-07-15       Impact factor: 3.857

9.  Presence of an endogenous superoxide dismutase activity in three rodent malaria species.

Authors:  P Bécuwe; C Slomianny; D Camus; D Dive
Journal:  Parasitol Res       Date:  1993       Impact factor: 2.289

10.  Purification of glutathionylspermidine and trypanothione synthetases from Crithidia fasciculata.

Authors:  K Smith; K Nadeau; M Bradley; C Walsh; A H Fairlamb
Journal:  Protein Sci       Date:  1992-07       Impact factor: 6.725

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