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

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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

Název v anglickém jazyce

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

Popis výsledku anglicky

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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Proteins-Structure, Function and Bioinformatics

ISSN

0887-3585

e-ISSN

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Svazek periodika

82

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

2552-2564

Kód UT WoS článku

000342849400022

EID výsledku v databázi Scopus

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