Literature DB >> 1594571

Increasing the thermostability of a neutral protease by replacing positively charged amino acids in the N-terminal turn of alpha-helices.

V G Eijsink1, G Vriend, B van den Burg, J R van der Zee, G Venema.   

Abstract

The 247-260 and 289-299 alpha-helices of Bacillus subtilis neutral protease have a lysine in their N-terminal turn. These lysines were replaced by Ser or Asp in order to improve electrostatic interactions with the alpha-helix dipole. After replacing Lys by Ser at positions 249 or 290, the thermostability of the enzyme was increased by 0.3 and 1.0 degrees C, respectively. The Asp249 and Asp290 mutants exhibited a stabilization of 0.6 and 1.2 degrees C, respectively. The results show the feasibility of stabilizing enzymes by introducing favourable residues at the end of alpha-helices.

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Year:  1992        PMID： 1594571     DOI： 10.1093/protein/5.2.165

Source DB:  PubMed          Journal:  Protein Eng        ISSN： 0269-2139


  7 in total

1.  In silico characterization of thermostable lipases.

Authors:  Debamitra Chakravorty; Saravanan Parameswaran; Vikash Kumar Dubey; Sanjukta Patra
Journal:  Extremophiles       Date:  2010-12-12       Impact factor: 2.395

Review 2.  The role of calcium ions in the stability and instability of a thermolysin-like protease.

Authors:  V G H Eijsink; B W Matthews; G Vriend
Journal:  Protein Sci       Date:  2011-07-11       Impact factor: 6.725

Review 3.  Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases.

Authors:  G Vriend; V Eijsink
Journal:  J Comput Aided Mol Des       Date:  1993-08       Impact factor: 3.686

4.  Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus.

Authors:  Renda Hawwa; John Aikens; Robert J Turner; Bernard D Santarsiero; Andrew D Mesecar
Journal:  Arch Biochem Biophys       Date:  2009-07-16       Impact factor: 4.013

5.  The sequence of a subtilisin-type protease (aerolysin) from the hyperthermophilic archaeum Pyrobaculum aerophilum reveals sites important to thermostability.

Authors:  P Völkl; P Markiewicz; K O Stetter; J H Miller
Journal:  Protein Sci       Date:  1994-08       Impact factor: 6.725

Review 6.  Molecular and biotechnological aspects of microbial proteases.

Authors:  M B Rao; A M Tanksale; M S Ghatge; V V Deshpande
Journal:  Microbiol Mol Biol Rev       Date:  1998-09       Impact factor: 11.056

7.  Improving the Efficiency of New Automatic Dishwashing Detergent Formulation by Addition of Thermostable Lipase, Protease and Amylase.

Authors:  Ashwini Naganthran; Malihe Masomian; Raja Noor Zaliha Raja Abd Rahman; Mohd Shukuri Mohamad Ali; Hisham Mohd Nooh
Journal:  Molecules       Date:  2017-09-19       Impact factor: 4.411
  7 in total

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