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Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase.
The covalent structure of the pig kidney fructose-1,6-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) subunit has been determined. Placement of the 335 amino acid residues in the polypeptide chain was based largely on automated Edman degradation of eight purified cyanogen bromide fragments generated from the S-carboxymethylated protein. The determination of the amino acid sequence of the largest cyanogen bromide fragment (154 residues) required additional analysis of subfragments obtained by tryptic cleavage at arginyl residues and by mild acid cleavage of an Asp-Pro peptide bond. Alignment of the cyanogen bromide fragments was accomplished by analysis of a product of limited proteolysis by an endogenous protease and by characterization of the tryptic peptides isolated from S-[14C]carboxymethylated fructose-1,6-bisphosphatase. This sequence information has permitted the identification of several reactive sites of functional and structural significance in pig kidney fructose-1,6-bisphosphatase.
PMID: 6296821 [PubMed - indexed for MEDLINE]
PMCID: PMC347298
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Cited by 14 PubMed Central articles
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Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity.
Lu G, Stec B, Giroux EL, Kantrowitz ER.
Protein Sci. 1996 Nov; 5(11):2333-42.
[Protein Sci. 1996]
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Crystal structure analyses of uncomplexed ecotin in two crystal forms: implications for its function and stability.
Shin DH, Song HK, Seong IS, Lee CS, Chung CH, Suh SW.
Protein Sci. 1996 Nov; 5(11):2236-47.
[Protein Sci. 1996]
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Crystal structures of the active site mutant (Arg-243-->Ala) in the T and R allosteric states of pig kidney fructose-1,6-bisphosphatase expressed in Escherichia coli.
Stec B, Abraham R, Giroux E, Kantrowitz ER.
Protein Sci. 1996 Aug; 5(8):1541-53.
[Protein Sci. 1996]
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