Molecular Mechanism of Mg-ATPase Activity

Molecular Mechanism of Mg-ATPase Activity Mg-ATPase is very important in living organisms. To better understand the molecular mechanism of Mg-ATPase activity, we applied the method of kinetic analysis of multi-sited enzyme systems; this is a suitable approach used for kinetic investigation of multi-sited enzyme systems. The study of Mg-ATPase has demonstrated: (1) It is a multi-sited enzyme system whose functional unit is minimum a dimmer; (2) Its substrate is MgATP, while free ATP and Mg2+ appear to be the enzyme modifiers with a dual effect; (3) The enzyme system for MgATP has at least three sites: i.e., the essential activator, full inhibitor, and partial effect modifiers sites; (4) Mg-ATPase carries out Mg2+ transport through the 1Mg2+:1ATP stochiometry. Based on the results of these analyses, the kinetic scheme for Mg-ATPase has been developed. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The Journal of Membrane Biology Springer Journals
Loading next page...
 
/lp/springer_journal/molecular-mechanism-of-mg-atpase-activity-qj306z6gSq
Publisher
Springer US
Copyright
Copyright © 2015 by Springer Science+Business Media New York
Subject
Life Sciences; Biochemistry, general; Human Physiology
ISSN
0022-2631
eISSN
1432-1424
D.O.I.
10.1007/s00232-014-9769-2
Publisher site
See Article on Publisher Site

Abstract

Mg-ATPase is very important in living organisms. To better understand the molecular mechanism of Mg-ATPase activity, we applied the method of kinetic analysis of multi-sited enzyme systems; this is a suitable approach used for kinetic investigation of multi-sited enzyme systems. The study of Mg-ATPase has demonstrated: (1) It is a multi-sited enzyme system whose functional unit is minimum a dimmer; (2) Its substrate is MgATP, while free ATP and Mg2+ appear to be the enzyme modifiers with a dual effect; (3) The enzyme system for MgATP has at least three sites: i.e., the essential activator, full inhibitor, and partial effect modifiers sites; (4) Mg-ATPase carries out Mg2+ transport through the 1Mg2+:1ATP stochiometry. Based on the results of these analyses, the kinetic scheme for Mg-ATPase has been developed.

Journal

The Journal of Membrane BiologySpringer Journals

Published: Jan 8, 2015

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off