PMID:9524204
| Citation |
Cornell, KA and Riscoe, MK (1998) Cloning and expression of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase: identification of the pfs gene product. Biochim. Biophys. Acta 1396:8-14 |
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| Abstract |
The enzyme 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (EC 3.2.2.9) is responsible for cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH). Based on amino acid sequence analysis of this enzyme from Klebsiella, we recently speculated that an open reading frame found in E. coli (designated pfs) encoded MTA/SAH nucleosidase. To explore this possibility, we amplified, cloned, and expressed the complete pfs gene from E. coli genomic DNA. The recombinant protein exhibited a molecular weight and Michaelis constants for MTA that are in agreement with those reported for native enzyme. From this biochemical evidence we confirm our original assignment of the pfs gene as encoding MTA/SAH nucleosidase. |
| Links | |
| Keywords |
Amino Acid Sequence; Base Sequence; Cloning, Molecular; DNA, Complementary/isolation & purification; Escherichia coli/genetics; Gene Expression Regulation, Bacterial; Genes, Bacterial; Molecular Sequence Data; N-Glycosyl Hydrolases/biosynthesis; N-Glycosyl Hydrolases/genetics; N-Glycosyl Hydrolases/isolation & purification; Polymerase Chain Reaction; Sequence Analysis, DNA; Sequence Homology, Amino Acid |
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