title: Engineering thermolysin-like proteases whose stability is largely independent of calcium.
abstract: Thermal stability of the thermolysin-like protease produced by Bacillus stearothermophilus (TLP-ste) is highly dependent on calcium at concentrations in the millimolar range. We describe the rational design and production of a fully active TLP-ste variant whose stability is only slightly dependent on calcium concentration.
authors.affiliation: Department of Genetics, University of Groningen, Haren, The Netherlands.
authors.forename: O R
authors.initials: OR
authors.lastname: Veltman
authors.forename: G
authors.initials: G
authors.lastname: Vriend
authors.forename: B
authors.initials: B
authors.lastname: van den Burg
authors.forename: F
authors.initials: F
authors.lastname: Hardy
authors.forename: G
authors.initials: G
authors.lastname: Venema
authors.forename: V G
authors.initials: VG
authors.lastname: Eijsink
mesh_terms: D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology*; D002135:Calcium-Binding Proteins / Q000187:drug effects / Q000235:genetics*; D004795:Enzyme Stability / Q000187:drug effects / Q000235:genetics; D006358:Hot Temperature; D011487:Protein Conformation; D011489:Protein Denaturation; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D013820:Thermolysin / Q000187:drug effects / Q000235:genetics*
chemical_list: D002135:Calcium-Binding Proteins; D013820:Thermolysin; D002118:Calcium