Hauptseite > Publikationsdatenbank > Thermostability of Irreversible Unfolding alpha-Amylases Analyzed by Unfolded Kinetics > print

001     49011
005     20200423204255.0
024 7 _ |a pmid:16150692
|2 pmid
024 7 _ |a 10.1074/jbc.M507530200
|2 DOI
024 7 _ |a WOS:000233044500009
|2 WOS
024 7 _ |a 2128/2652
|2 Handle
037 _ _ |a PreJuSER-49011
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Duy, C.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB58067
245 _ _ |a Thermostability of Irreversible Unfolding alpha-Amylases Analyzed by Unfolded Kinetics
260 _ _ |a Bethesda, Md.
|b Soc.
|c 2005
300 _ _ |a 37360 - 37365
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
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 Journal of Biological Chemistry
|x 0021-9258
|0 3091
|v 280
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a For most multidomain proteins the thermal unfolding transitions are accompanied by an irreversible step, often related to aggregation at elevated temperatures. As a consequence the analysis of thermostabilities in terms of equilibrium thermodynamics is not applicable, at least not if the irreversible process is fast with respect the structural unfolding transition. In a comparative study we investigated aggregation effects and unfolding kinetics for five homologous alpha-amylases, all from mesophilic sources but with rather different thermostabilities. The results indicate that for all enzymes the irreversible process is fast and the precedent unfolding transition is the rate-limiting step. In this case the kinetic barrier toward unfolding, as measured by unfolding rates as function of temperature, is the key feature in thermostability. The investigated enzymes exhibit activation energies (E(a)) between 208 and 364 kJmol(-1) and pronounced differences in the corresponding unfolding rates. The most thermostable alpha-amylase from Bacillus licheniformis (apparent transition temperature, T(1/2) approximately 100 degrees C) shows an unfolding rate which is four orders of magnitude smaller as compared with the alpha-amylase from pig pancreas (T(1/2) approximately 65 degrees C). Even with respect to two other alpha-amylases from Bacillus species (T(1/2) approximately 86 degrees C) the difference in unfolding rates is still two orders of magnitude.
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 Animals
650 _ 2 |2 MeSH
|a Aspergillus oryzae: enzymology
650 _ 2 |2 MeSH
|a Bacillus: enzymology
650 _ 2 |2 MeSH
|a Circular Dichroism
650 _ 2 |2 MeSH
|a Enzyme Stability
650 _ 2 |2 MeSH
|a Hot Temperature
650 _ 2 |2 MeSH
|a Kinetics
650 _ 2 |2 MeSH
|a Protein Denaturation
650 _ 2 |2 MeSH
|a Protein Folding
650 _ 2 |2 MeSH
|a Swine
650 _ 2 |2 MeSH
|a Thermodynamics
650 _ 2 |2 MeSH
|a Transition Temperature
650 _ 2 |2 MeSH
|a alpha-Amylases: chemistry
650 _ 2 |2 MeSH
|a alpha-Amylases: metabolism
650 _ 7 |0 EC 3.2.1.1
|2 NLM Chemicals
|a alpha-Amylases
650 _ 7 |a J
|2 WoSType
700 1 _ |a Fitter, J.
|b 1
|u FZJ
|0 P:(DE-Juel1)131961
773 _ _ |a 10.1074/jbc.M507530200
|g Vol. 280, p. 37360 - 37365
|p 37360 - 37365
|q 280<37360 - 37365
|0 PERI:(DE-600)1474604-9
|t The @journal of biological chemistry
|v 280
|y 2005
|x 0021-9258
856 7 _ |u http://dx.doi.org/10.1074/jbc.M507530200
|u http://hdl.handle.net/2128/2652
856 4 _ |u https://juser.fz-juelich.de/record/49011/files/76868.pdf
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/49011/files/76868.jpg?subformat=icon-1440
|x icon-1440
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/49011/files/76868.jpg?subformat=icon-180
|x icon-180
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/49011/files/76868.jpg?subformat=icon-640
|x icon-640
|y OpenAccess
909 C O |o oai:juser.fz-juelich.de:49011
|p openaire
|p open_access
|p driver
|p VDB
|p dnbdelivery
913 1 _ |k L01
|v Neurowissenschaften
|l Funktion und Dysfunktion des Nervensystems
|b Leben
|0 G:(DE-Juel1)FUEK255
|x 0
914 1 _ |y 2005
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
915 _ _ |2 StatID
|0 StatID:(DE-HGF)0510
|a OpenAccess
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
|x 0
970 _ _ |a VDB:(DE-Juel1)76868
980 1 _ |a FullTexts
980 _ _ |a VDB
980 _ _ |a JUWEL
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
980 _ _ |a FullTexts
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21