Specific potassium ion interactions facilitate homocysteine binding to betaine-homocysteine S-methyltransferase

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00435073" target="_blank" >RIV/61388963:_____/14:00435073 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1002/prot.24619" target="_blank" >http://dx.doi.org/10.1002/prot.24619</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/prot.24619" target="_blank" >10.1002/prot.24619</a>

Result language
angličtina
Original language name
Specific potassium ion interactions facilitate homocysteine binding to betaine-homocysteine S-methyltransferase
Original language description
Betaine-homocysteine S-methyltransferase (BHMT) is a zinc-dependent methyltransferase that uses betaine as the methyl donor for the remethylation of homocysteine to form methionine. This reaction supports S-adenosylmethionine biosynthesis, which is required for hundreds of methylation reactions in humans. Herein we report that BHMT is activated by potassium ions with an apparent K-M for K+ of about 100 mu M. The presence of potassium ions lowers the apparent K-M of the enzyme for homocysteine, but it does not affect the apparent K-M for betaine or the apparent k(cat) for either substrate. We employed molecular dynamics (MD) simulations to theoretically predict and protein crystallography to experimentally localize the binding site(s) for potassium ion(s). Simulations predicted that K+ ion would interact with residues Asp26 and/or Glu159. Our crystal structure of BHMT bound to homocysteine confirms these sites of interaction and reveals further contacts between K+ ion and BHMT residues
Czech name
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Czech description
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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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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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