Abstract
A full-length clone of pig kidney fructose 1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) was isolated by screening a cDNA library for complementation of an Escherichia coli fbp deletion mutation. The open reading frame of 1011 bases corresponds to 337 amino acids, two more than have been previously reported [Marcus, F., Edelstein, I., Reardon, I. & Heinrikson, R. L. (1982) Proc. Natl. Acad. Sci. USA 79, 7161-7165]. The extra two amino acids (Ala-Lys) are located at the C-terminal end of the protein as an extension. Comparison of the deduced amino acid sequence with the reported (see above) and revised amino acid sequence [Harrsch, P. B., Kim, Y., Fox, J. L. & Marcus, F. (1985) Biochem. Biophys. Res. Commun. 133, 520-526] indicates three differences in addition to the C-terminal extension. Gln-20, Thr-96, and Asn-199 in the amino acid sequence are found to be Glu, Ser, and Asp, respectively. Since the x-ray structure of the pig kidney enzyme has been reported, the cDNA clone will allow the construction of site-specific mutants to help test possible structure-function relationships in this important metabolic enzyme.
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