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  • Title: Characterization of the genes for fructose-bisphosphate aldolase in Trypanosoma brucei.
    Author: Marchand M, Poliszczak A, Gibson WC, Wierenga RK, Opperdoes FR, Michels PA.
    Journal: Mol Biochem Parasitol; 1988 May; 29(1):65-75. PubMed ID: 3386689.
    Abstract:
    In Trypanosoma brucei stock 427 the glycolytic enzyme fructose-bisphosphate aldolase is encoded by two tandemly linked genes of identical sequence. Such a tandem arrangement of aldolase genes is also present in other T. brucei stocks of unrelated origin. In stock 427 one of the allelic genes is a pseudogene, as a result of a one-nucleotide deletion. The genes code for a polypeptide of 371 amino acids, with a calculated molecular weight of 40,940. The protein that is predicted from the gene sequence has 45-48% positional identity with known aldolase sequences of other organisms. The trypanosomal protein is, however, unique in having a 10 amino-acid insertion near its N-terminus and high number of basic residues, a feature it shares with other glycolytic enzymes of T. brucei. These glycolytic enzymes have in common that they are located in microbody-like organelles, the glycosomes. We have previously proposed that the positively charged residues may be involved in the import of the proteins into the organelles.
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