Conserved residues of liquefying α-amylases are concentrated in the vicinity of active site
- 1 January 1990
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 166 (1), 61-65
- https://doi.org/10.1016/0006-291x(90)91911-b
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Regional distant sequence homology between amylases, α‐glucosidases and transglucanosylasesFEBS Letters, 1988
- Extracellular production of cloned α-amylase by Escherichia coliGene, 1987
- Complete Nucleotide Sequence of a Gene Coding for Heat- and pH-Stable α-Amylase of Bacillus licheniformis: Comparison of the Amino Acid Sequences of Three Bacterial Liquefying α-Amylases Deduced from the DNA Sequences1The Journal of Biochemistry, 1985
- Conserved amino acid sequence domains in alpha-amylases from plants, mammals, and bacteriaBiochemical and Biophysical Research Communications, 1985
- Critical evaluation of comparative model building of Streptomyces griseus trypsinBiochemistry, 1984
- Structure and Possible Catalytic Residues of Taka-Amylase AThe Journal of Biochemistry, 1984
- A graphics model building and refinement system for macromoleculesJournal of Applied Crystallography, 1978
- A general method applicable to the search for similarities in the amino acid sequence of two proteinsJournal of Molecular Biology, 1970