Fructose 1,6-bisphosphate aldolase of Drosophila melanogaster: Comparative sequence analyses around the substrate-binding lysyl residue
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference39 articles.
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1. Amino Acid Sequence around the Active Site of Two Class I Fructose-1,6-Bisphosphate Aldolases from Staphylococci;European Journal of Biochemistry;2005-03-03
2. The three-dimensional structure of N -acetylneuraminate lyase from Escherichia coli;Structure;1994-05
3. Cloning, sequencing, and characterization of the gene encoding the class I fructose-1,6-bisphosphate aldolase of Staphylococcus carnosus;Journal of Bacteriology;1993-11
4. The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogasterat 2.5A˚resolution;FEBS Letters;1991-11-04
5. Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster: Primary structure analysis, secondary structure prediction, and comparison with vertebrate aldolases;Archives of Biochemistry and Biophysics;1988-10
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