Rabbit liver fructose-1,6-bisphosphatase: Location of an active site lysyl residue in the COOH-terminal fragment generated by a lysosomal proteinase
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. Evidence for the selective release of lysosomal proteinases in fasted rabbits
2. Transformation of neutral to alkaline fructose 1,6-bisphosphatase
3. Modification of fructose bisphosphatase by a proteolytic enzyme from rat liver lysosomes
4. 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
5. The carboxy-terminal amino acid sequence of rabbit liver fructose 1,6-bisphosphatase
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1. Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 Å resolution;Acta Crystallographica Section D Biological Crystallography;1999-01-01
2. Site-directed mutagenesis shows that lysine-299 is essential for activity of pea chloroplast fructose-1,6-bisphosphatase;Plant Science;1995-03
3. Modification of cys-128 of pig kidney fructose 1,6-bisphosphatase with different thiol reagents: Size dependent effect on the substrate and fructose-2,6-bisphosphate interaction;Journal of Protein Chemistry;1993-04
4. Plant fructose-1,6-bisphosphatases: characteristics and properties;International Journal of Biochemistry;1992-08
5. Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution.;Proceedings of the National Academy of Sciences;1991-04-15
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