Subunit?subunit interactions are weakened in mutant forms of acetohydroxy acid synthase insensitive to valine inhibition
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F10%3A00340830" target="_blank" >RIV/61388971:_____/10:00340830 - isvavai.cz</a>
Alternative codes found
RIV/00027006:_____/10:00001336
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Subunit?subunit interactions are weakened in mutant forms of acetohydroxy acid synthase insensitive to valine inhibition
Original language description
In acetohydroxy acid synthase from Streptomyces cinnamonensis mutants aVected in valine regulation, the impact of mutations on interactions between the catalytic and the regulatory subunits was examined using yeast twohybrid system. Mutations in the catalytic and the regulatory subunits were projected into homology models of the respective proteins. Two changes in the catalytic subunit, E139A (domain) and Q217 (domain), both located on the surface of the catalytic subunit dimer, lowered the interactionwith the regulatory subunit. Three consecutive changes in the N-terminal part of the regulatory subunit were examined
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Archives of Microbiology
ISSN
0302-8933
e-ISSN
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Volume of the periodical
192
Issue of the periodical within the volume
3
Country of publishing house
DE - GERMANY
Number of pages
6
Pages from-to
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UT code for WoS article
00274455600006
EID of the result in the Scopus database
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