Cross-Talk between the Catalytic Core and the Regulatory Domain in Cystathionine beta-Synthase: Study by Differential Covalent Labeling and Computational Modeling
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F10%3A7639" target="_blank" >RIV/00216208:11110/10:7639 - isvavai.cz</a>
Alternative codes found
RIV/60461373:22330/10:00024202 RIV/00064165:_____/10:7639
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Cross-Talk between the Catalytic Core and the Regulatory Domain in Cystathionine beta-Synthase: Study by Differential Covalent Labeling and Computational Modeling
Original language description
Cystathionine ?-synthase (CBS) is a modular enzyme which catalyzes condensation of serine with homocysteine. The atomic mechanisms of the CBS allostery have not yet been sufficiently explained. To determine the contact area between the catalytic core andthe autoinhibitory module of the CBS protein, we compared side-chain reactivity of the truncated CBS lacking the regulatory domain (45CBS) and of the full-length enzyme (wtCBS) using covalent labeling by six different modification agents and subsequentmass spectrometry. Fifty modification sites were identified in 45CBS, and four of them were not labeled in wtCBS. One differentially reactive site (cluster W408/W409/W410) is a part of the linker between the domains. The other three residues (K172 and/orK177, R336, and K384) are located in the same region of the 45CBS crystal structure; computational modeling showed that these amino acid side chains potentially form a regulatory interface in CBS protein.
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
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
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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
Biochemistry
ISSN
0006-2960
e-ISSN
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Volume of the periodical
49
Issue of the periodical within the volume
49
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
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UT code for WoS article
000284975000018
EID of the result in the Scopus database
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