All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

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

The result's identifiers

  • Result code in 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>

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GA15-19883S" target="_blank" >GA15-19883S: Molecular mechanisms of intraprotein/interdomain signal transduction in model heme sensor proteins</a><br>

  • Continuities

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

Others

  • Publication year

    2015

  • 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

  • Volume of the periodical

    54

  • Issue of the periodical within the volume

    32

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    13

  • Pages from-to

    5017-5029

  • UT code for WoS article

    000359892300007

  • EID of the result in the Scopus database

    2-s2.0-84939630418