Kinetic Analysis of a Globin-Coupled Histidine Kinase, AfGcHK: Effects of the Heme Iron Complex, Response Regulator, and Metal Cations on Autophosphorylation Activity

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10314838" target="_blank" >RIV/00216208:11310/15:10314838 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1021/acs.biochem.5b00517" target="_blank" >http://dx.doi.org/10.1021/acs.biochem.5b00517</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.biochem.5b00517" target="_blank" >10.1021/acs.biochem.5b00517</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Kinetic Analysis of a Globin-Coupled Histidine Kinase, AfGcHK: Effects of the Heme Iron Complex, Response Regulator, and Metal Cations on Autophosphorylation Activity

Popis výsledku v původním jazyce

The globin-coupled histidine kinase, AfGcHK, is a part of the two-component signal transduction system from the soil bacterium Anaeromyxobacter sp. Fw109-5. Activation of its sensor domain significantly increases its autophosphorylation activity, which targets the His183 residue of its functional domain. The phosphate group of phosphorylated AfGcHK is then transferred to the cognate response regulator. We investigated the effects of selected variables on the autophosphorylation reaction's kinetics. Thek(cat) values of the heme Fe(III)-OH-, Fe(III)-cyanide, Fe(III)-imidazole, and Fe(II)-O-2 bound active AfGcHK forms were 1.1-1.2 min(-1), and their K-m(ATP) values were 18.9-35.4 mu M. However, the active form bearing a CO-bound Fe(II) heme had a k(cat)of 1.0 min(-1) but a very high K-m(ATP) value of 357 mu M, suggesting that its active site structure differs strongly from the other active forms. The Fe(II) heme-bound inactive form had k(cat) and K-m(ATP) values of 0.4 min(-1) and 78 mu

Název v anglickém jazyce

Kinetic Analysis of a Globin-Coupled Histidine Kinase, AfGcHK: Effects of the Heme Iron Complex, Response Regulator, and Metal Cations on Autophosphorylation Activity

Popis výsledku anglicky

The globin-coupled histidine kinase, AfGcHK, is a part of the two-component signal transduction system from the soil bacterium Anaeromyxobacter sp. Fw109-5. Activation of its sensor domain significantly increases its autophosphorylation activity, which targets the His183 residue of its functional domain. The phosphate group of phosphorylated AfGcHK is then transferred to the cognate response regulator. We investigated the effects of selected variables on the autophosphorylation reaction's kinetics. Thek(cat) values of the heme Fe(III)-OH-, Fe(III)-cyanide, Fe(III)-imidazole, and Fe(II)-O-2 bound active AfGcHK forms were 1.1-1.2 min(-1), and their K-m(ATP) values were 18.9-35.4 mu M. However, the active form bearing a CO-bound Fe(II) heme had a k(cat)of 1.0 min(-1) but a very high K-m(ATP) value of 357 mu M, suggesting that its active site structure differs strongly from the other active forms. The Fe(II) heme-bound inactive form had k(cat) and K-m(ATP) values of 0.4 min(-1) and 78 mu

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GA15-19883S" target="_blank" >GA15-19883S: Mechanismus intraproteinového/mezidoménového přenosu signálu u modelových hemových senzorových proteinů</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Biochemistry

ISSN

0006-2960

e-ISSN

—

Svazek periodika

54

Číslo periodika v rámci svazku

32

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

5017-5029

Kód UT WoS článku

000359892300007

EID výsledku v databázi Scopus

2-s2.0-84939630418