Location of lysyl residues at the allosteric site of fructose 1,6-bisphosphatase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference10 articles.
1. Rabbit liver fructose 1,6-bisphosphatase: Labeling of the active and allosteric sites with pyridoxal 5-phosphate and sequence of a nonapeptide from the active site
2. Modification of fructose-1,6-diphosphatase with pyridoxal 5'-phosphate. Evidence for the participation of lysyl residues at the activesite
3. On the nucleotide binding domain of fructose-1,6-bisphosphatase
4. Rabbit liver fructose-1,6-bisphosphatase: Location of an active site lysyl residue in the COOH-terminal fragment generated by a lysosomal proteinase
5. Digestion of rabbit liver fructose 1,6-bisphosphatase with subtilisin: Sites of cleavage and activity of the modified enzyme
Cited by 15 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 Å resolution;Acta Crystallographica Section D Biological Crystallography;1999-01-01
2. Suppression of kinetic AMP cooperativity of fructose-1,6-bisphosphatase by carbamoylation of lysine 50;Journal of Protein Chemistry;1999
3. Site-directed mutagenesis shows that lysine-299 is essential for activity of pea chloroplast fructose-1,6-bisphosphatase;Plant Science;1995-03
4. Lysine 274 is essential for fructose 2,6-bisphosphate inhibition of fructose-1,6-bisphosphatase.;Journal of Biological Chemistry;1992-04
5. Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium.;Proceedings of the National Academy of Sciences;1990-07-01
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