Identification of zinc‐binding ligands in the Class II fructose‐ 1,6‐bisphosphate aldolase of Escherichia coli

[1]  J. Sambrook,et al.  Molecular Cloning: A Laboratory Manual , 2001 .

[2]  K. Piontek,et al.  The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution , 1993, FEBS letters.

[3]  J. Marsh,et al.  Fructose-bisphosphate aldolases: an evolutionary history. , 1992, Trends in biochemical sciences.

[4]  J. Haeggström,et al.  Leukotriene A4 hydrolase: determination of the three zinc-binding ligands by site-directed mutagenesis and zinc analysis. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[5]  F. Tabita,et al.  Nucleotide sequence, transcriptional analysis, and expression of genes encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides. , 1991, The Journal of biological chemistry.

[6]  G J Davies,et al.  Activity and specificity of human aldolases. , 1991, Journal of molecular biology.

[7]  B. Vallee,et al.  Zinc coordination, function, and structure of zinc enzymes and other proteins. , 1990, Biochemistry.

[8]  Gregory A. Petsko,et al.  The evolution of a/ barrel enzymes , 1990 .

[9]  R. Perham The fructose-1,6-bisphosphate aldolases: same reaction, different enzymes. , 1990, Biochemical Society transactions.

[10]  H. Watson,et al.  The crystal structure of human muscle aldolase at 3.0 Å resolution , 1990, FEBS letters.

[11]  C. Barbas,et al.  Molecular cloning, nucleotide sequence and fine‐structural analysis of the Corynebacterium glutamicum fda gene: structural comparison of C. glutamicum fructose‐1,6‐biphosphate aldolase to class I and class II aldolases , 1989, Molecular microbiology.

[12]  L. Ingram,et al.  Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae , 1989, Journal of bacteriology.

[13]  S. Kohlwein,et al.  Molecular cloning, primary structure and disruption of the structural gene of aldolase from Saccharomyces cerevisiae. , 1989, European journal of biochemistry.

[14]  S. Baldwin,et al.  Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli. , 1989, The Biochemical journal.

[15]  M. Allaire,et al.  Molecular architecture of rabbit skeletal muscle aldolase at 2.7-A resolution. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[16]  F. Eckstein,et al.  The use of phosphorothioate-modified DNA in restriction enzyme reactions to prepare nicked DNA. , 1985, Nucleic acids research.

[17]  P. Henderson,et al.  Location of a structural gene for xylose-H+ symport at 91 min on the linkage map of Escherichia coli K12. , 1984, The Journal of biological chemistry.

[18]  J. Devereux,et al.  A comprehensive set of sequence analysis programs for the VAX , 1984, Nucleic Acids Res..

[19]  M. Hatada,et al.  Comparison of the folding of 2-keto-3-deoxy-6-phosphogluconate aldolase, triosephosphate isomerase and pyruvate kinase. Implications in molecular evolution. , 1982, Journal of molecular biology.

[20]  M. Hatada,et al.  Structure of 2-keto-3-deoxy-6-phosphogluconate aldolase at 2 . 8 A resolution. , 1978, Journal of molecular biology.

[21]  S. Baldwin,et al.  Purification and characterization of the class-II D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain). , 1978, The Biochemical journal.

[22]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[23]  F. C. Hartman,et al.  Affinity labeling of yeast aldolase by haloacetol phosphates. , 1971, Biochemical and biophysical research communications.

[24]  W. Rutter,et al.  Magnetic resonance studies of the role of the divalent cation in the mechanism of yeast aldolase. , 1971, Biochemistry.

[25]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[26]  Ingram Jm Fructose diphosphate aldolase of yeast: studies on the sulfhydryl groups. , 1969 .

[27]  W. Rutter,et al.  COMPARATIVE STUDIES OF LIVER AND MUSCLE ALDOLASE. II. IMMUNOCHEMICAL AND CHROMATOGRAPHIC DIFFERENTIATION. , 1963, The Journal of biological chemistry.

[28]  J. Lederberg,et al.  Concentration of biochemical mutants of bacteria with penicillin. , 1948, Journal of the American Chemical Society.

[29]  W. Cleland,et al.  The statistical analysis of enzyme kinetic data. , 1967, Advances in enzymology and related areas of molecular biology.

[30]  American Crystallographic Association , 1950, Nature.