3-Mercaptopyruvate sulfurtransferase of Leishmania contains an unusual C-terminal extension and is involved in thioredoxin and antioxidant metabolism

Journal of Biological Chemistry

Volumn 278, Issue 3, 2003, Pages 1480-1486

  Williams, Roderick A M ^a   Kelly, Sharon M ^a   Mottram, Jeremy C ^b   Coombs, Graham H ^a,b  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIOXIDANTS; ENZYMES; METABOLISM; OXIDATION;

OXIDATIVE STRESS;

CLONING;

3 MERCAPTOPYRUVATE SULFURTANSFERASE; 3 MERCAPTOPYRUVIC ACID; ANTIOXIDANT; CYANIDE; IRON SULFUR PROTEIN; RECOMBINANT ENZYME; SULFANE; SULFUR AMINO ACID; SULFUR DERIVATIVE; SULFURTRANSFERASE; THIOCYANATE; THIOREDOXIN; THIOSULFATE; UNCLASSIFIED DRUG; 3 MERCAPTOPYRUVATE SULPHURTRANSFERASE; 3-MERCAPTOPYRUVATE SULPHURTRANSFERASE; PRIMER DNA; RECOMBINANT PROTEIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE; GENE SEQUENCE; GENE STRUCTURE; GENETIC CODE; LEISHMANIA; LEISHMANIA MAJOR; LEISHMANIA MEXICANA; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; SEQUENCE HOMOLOGY; STRESS; TRYPANOSOMA BRUCEI; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; POLYMERASE CHAIN REACTION; PROTEIN DENATURATION;

ESCHERICHIA COLI; LEISHMANIA MAJOR; LEISHMANIA MEXICANA; PROTOZOA; TRYPANOSOMA; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI;

AMINO ACID SEQUENCE; ANIMALS; ANTIOXIDANTS; BASE SEQUENCE; CLONING, MOLECULAR; DNA PRIMERS; LEISHMANIA MAJOR; LEISHMANIA MEXICANA; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; POLYMERASE CHAIN REACTION; PROTEIN DENATURATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SULFURTRANSFERASES; THIOREDOXIN;

EID: 0037449796     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M209395200     Document Type: Article

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