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Literature DB >> 1637352

Increasing the thermostability of the neutral proteinase of Bacillus stearothermophilus by improvement of internal hydrogen-bonding.

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

Abstract

In an attempt to increase the thermostability of the neutral proteinase of Bacillus stearothermophilus the buried Ala-170 was replaced by serine. Molecular-dynamics simulations showed that Ser-170 stabilizes the enzyme by formation of an internal hydrogen bond. In addition, the hydroxy group of Ser-170 could contribute to stability by filling an internal cavity. After the introduction of the mutation, using site-directed-mutagenesis techniques, an increase in stability of 0.7 +/- 0.1 degrees C was obtained.

Entities: Chemical Mutation Species

Mesh：

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Year: 1992 PMID： 1637352 PMCID： PMC1132834 DOI： 10.1042/bj2850625

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

26 in total

1. WHAT IF: a molecular modeling and drug design program.

Authors: G Vriend
Journal: J Mol Graph Date: 1990-03

2. One-step affinity purification of Bacillus neutral proteases using bacitracin-silica.

Authors: B Van Den Burg; V G Eijsink; B K Stulp; G Venema
Journal: J Biochem Biophys Methods Date: 1989-05

3. Neutral proteases of the genus Bacillus.

Authors: L Keay
Journal: Biochem Biophys Res Commun Date: 1969-07-23 Impact factor: 3.575

4. A new way of enhancing the thermostability of proteases.

Authors: T Imanaka; M Shibazaki; M Takagi
Journal: Nature Date: 1986 Dec 18-31 Impact factor: 49.962

5. Contribution of the C-terminal amino acid to the stability of Bacillus subtilis neutral protease.

Authors: V G Eijsink; G Vriend; B Van Den Burg; G Venema; B K Stulp
Journal: Protein Eng Date: 1990-10

6. Improving the thermostability of the neutral protease of Bacillus stearothermophilus by replacing a buried asparagine by leucine.

Authors: V G Eijsink; J R van der Zee; B van den Burg; G Vriend; G Venema
Journal: FEBS Lett Date: 1991-04-22 Impact factor: 4.124

7. Thermostability of Bacillus subtilis neutral protease.

Authors: V G Eijsink; B van den Burg; G Vriend; H J Berendsen; G Venema
Journal: Biochem Int Date: 1991-06

8. Grafting of a calcium-binding loop of thermolysin to Bacillus subtilis neutral protease.

Authors: S Toma; S Campagnoli; I Margarit; R Gianna; G Grandi; M Bolognesi; V De Filippis; A Fontana
Journal: Biochemistry Date: 1991-01-08 Impact factor: 3.162

9. Stabilization of the neutral protease of Bacillus stearothermophilus by removal of a buried water molecule.

Authors: G Vriend; H J Berendsen; J R van der Zee; B van den Burg; G Venema; V G Eijsink
Journal: Protein Eng Date: 1991-12

10. Crystal structure of neutral protease from Bacillus cereus refined at 3.0 A resolution and comparison with the homologous but more thermostable enzyme thermolysin.

Authors: R A Pauptit; R Karlsson; D Picot; J A Jenkins; A S Niklaus-Reimer; J N Jansonius
Journal: J Mol Biol Date: 1988-02-05 Impact factor: 5.469

4 in total

4. RankProt: A multi criteria-ranking platform to attain protein thermostabilizing mutations and its in vitro applications - Attribute based prediction method on the principles of Analytical Hierarchical Process.

Authors: Debamitra Chakravorty; Sanjukta Patra
Journal: PLoS One Date: 2018-10-04 Impact factor: 3.240