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Titolo:
ISOLATION AND SEQUENCE-ANALYSIS OF THE CDNA FOR PIG-KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE
Autore:
WILLIAMS MK; KANTROWITZ ER;
Indirizzi:
BOSTON COLL,DEPT CHEM CHESTNUT HILL MA 02167
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 7, volume: 89, anno: 1992,
pagine: 3080 - 3082
SICI:
0027-8424(1992)89:7<3080:IASOTC>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; FRUCTOSE-1,6-BISPHOSPHATASE; BISPHOSPHATASE; GENE; DNA;
Keywords:
AMINO ACID SEQUENCE; ALLOSTERIC ENZYME;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
19
Recensione:
Indirizzi per estratti:
Citazione:
M.K. Williams e E.R. Kantrowitz, "ISOLATION AND SEQUENCE-ANALYSIS OF THE CDNA FOR PIG-KIDNEY FRUCTOSE 1,6-BISPHOSPHATASE", Proceedings of the National Academy of Sciences of the United Statesof America, 89(7), 1992, pp. 3080-3082

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 byscreening a cDNA library for complementation of an Escherichia coli fbp deletion mutation. The open reading frame of 1011 bases correspondsto 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/10/20 alle ore 08:27:03