Transketolase from Leishmania mexicana has a dual subcellular localization.
Biochem J
; 382(Pt 2): 759-67, 2004 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-15149284
Transketolase has been characterized in Leishmania mexicana. A gene encoding this enzyme was identified and cloned. The gene was expressed in Escherichia coli and the protein was purified and characterized. An apparent K(m) of 2.75 mM for ribose 5-phosphate was determined. X-ray crystallography was used to determine the three-dimensional structure of the enzyme to a resolution of 2.2 A (1 A identical with 0.1 nm). The C-terminus of the protein contains a type-1 peroxisome-targeting signal, suggestive of a possible glycosomal subcellular localization. Subcellular localization experiments performed with promastigote forms of the parasite revealed that the protein was predominantly cytosolic, although a significant component of the total activity was associated with the glycosomes. Transketolase is thus the first enzyme of the nonoxidative branch of the pentose phosphate pathway whose presence has been demonstrated in a peroxisome-like organelle.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Transcetolase
/
Leishmania mexicana
Limite:
Animals
País/Região como assunto:
Mexico
Idioma:
En
Revista:
Biochem J
Ano de publicação:
2004
Tipo de documento:
Article
País de publicação:
Reino Unido