Hauptseite > Publikationsdatenbank > Structural Stability and Unfolding Properties of Thermostable bacterial alpha-amylases: A Comparative Study on Homologous Enzymes > print

001     42202
005     20200423203937.0
024 7 _ |a pmid:15274613
|2 pmid
024 7 _ |a 10.1021/bi0493362
|2 DOI
024 7 _ |a WOS:000222965100002
|2 WOS
024 7 _ |a 2128/701
|2 Handle
037 _ _ |a PreJuSER-42202
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Fitter, J.
|b 0
|u FZJ
|0 P:(DE-Juel1)131961
245 _ _ |a Structural Stability and Unfolding Properties of Thermostable bacterial alpha-amylases: A Comparative Study on Homologous Enzymes
260 _ _ |a Columbus, Ohio
|b American Chemical Society
|c 2004
300 _ _ |a 9589 - 9599
336 7 _ |a Journal Article
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|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
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336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Biochemistry
|x 0006-2960
|0 798
|v 43
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a In a comparative investigation on two thermostable alpha-amylases [Bacillus amyloliquefaciens (BAA), T(m) = 86 degrees C and Bacillus licheniformis (BLA), T(m) = 101 degrees C], we studied thermal and guanidine hydrochloride (GndHCl)-induced unfolding using fluorescence and CD spectroscopy, as well as dynamic light scattering. Depletion of calcium from specific ion-binding sites in the protein structures reduces the melting temperature tremendously for both alpha-amylases. The reduction is nearly the same for both enzymes, namely, in the order of 50 degrees C. Thus, the difference in thermostability between BLA and BAA (DeltaT(m) approximately 15 degrees C) is related to intrinsic properties of the respective protein structures themselves and is not related to the strength of ion binding. The thermal unfolding of both proteins is characterized by a full disappearance of secondary structure elements and by a concurrent expansion of the 3D structure. GndHCl-induced unfolding also yields a fully vanishing secondary structure but with more expanded 3D structures. Both alpha-amylases remain much more compact upon thermal unfolding as compared to the fully unfolded state induced by chemical denaturants. Such rather compact thermal unfolded structures lower the conformational entropy change during the unfolding transition, which principally can contribute to an increased thermal stability. Structural flexibilities of both enzymes, as measured with tryptophan fluorescence quenching, are almost identical for both enzymes in the native states, as well as in the unfolded states. Furthermore, we do not observe any difference in the temperature dependence of the structural flexibilities between BLA and BAA. These results indicate that conformational dynamics on the time scale of our studies seem not to be related to thermal stability or to thermal adaptation.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK255
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Bacillus: enzymology
650 _ 2 |2 MeSH
|a Bacterial Proteins: chemistry
650 _ 2 |2 MeSH
|a Enzyme Stability
650 _ 2 |2 MeSH
|a Guanidine: chemistry
650 _ 2 |2 MeSH
|a Kinetics
650 _ 2 |2 MeSH
|a Light
650 _ 2 |2 MeSH
|a Protein Denaturation
650 _ 2 |2 MeSH
|a Protein Folding
650 _ 2 |2 MeSH
|a Scattering, Radiation
650 _ 2 |2 MeSH
|a Sequence Homology, Amino Acid
650 _ 2 |2 MeSH
|a Spectrometry, Fluorescence
650 _ 2 |2 MeSH
|a Temperature
650 _ 2 |2 MeSH
|a Thermodynamics
650 _ 2 |2 MeSH
|a alpha-Amylases: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a Bacterial Proteins
650 _ 7 |0 113-00-8
|2 NLM Chemicals
|a Guanidine
650 _ 7 |0 EC 3.2.1.1
|2 NLM Chemicals
|a alpha-Amylases
650 _ 7 |a J
|2 WoSType
700 1 _ |a Haber-Pohlmeier, S.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB12272
773 _ _ |a 10.1021/bi0493362
|g Vol. 43, p. 9589 - 9599
|p 9589 - 9599
|q 43<9589 - 9599
|0 PERI:(DE-600)1472258-6
|t Biochemistry
|v 43
|y 2004
|x 0006-2960
856 7 _ |u http://dx.doi.org/10.1021/bi0493362
|u http://hdl.handle.net/2128/701
856 4 _ |u https://juser.fz-juelich.de/record/42202/files/58752.pdf
|y OpenAccess
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