1au9: Difference between revisions
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Revision as of 15:46, 30 October 2007
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SUBTILISIN BPN' MUTANT 8324 IN CITRATE
OverviewOverview
Six individual amino acid substitutions at separate positions in the, tertiary structure of subtilisin BPN' (EC 3.4.21.14) were found to, increase the stability of this enzyme, as judged by differential scanning, calorimetry and decreased rates of thermal inactivation. These stabilizing, changes, N218S, G169A, Y217K, M50F, Q206C, and N76D, were discovered, through the use of five different investigative approaches: (1) random, mutagenesis; (2) design of buried hydrophobic side groups; (3) design of, electrostatic interactions at Ca2+ binding sites; (4) sequence homology, consensus; and (5) serendipity. Individually, the six amino acid, substitutions increase the delta G of unfolding between 0.3 and 1.3, kcal/mol at 58.5 degrees C. The combination of these six individual, stabilizing ... [(full description)]
About this StructureAbout this Structure
1AU9 is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens] with CA, UNX and IPA as [ligands]. Active as [Subtilisin], with EC number [3.4.21.62]. Structure known Active Sites: 169, 206, 217, 218, C22, C87, CA1, CA2 and F50. Full crystallographic information is available from [OCA].
ReferenceReference
Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding., Pantoliano MW, Whitlow M, Wood JF, Dodd SW, Hardman KD, Rollence ML, Bryan PN, Biochemistry. 1989 Sep 5;28(18):7205-13. PMID:2684274
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