Document Detail


Tyr-341 of the beta subunit is a major Km-determining residue of TF1-ATPase: parallel effect of its mutations on Kd(ATP) of the beta subunit and on Km(ATP) of the alpha 3 beta 3 gamma complex.
MedLine Citation:
PMID:  8089097     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Residue Tyr-341 of the F1-ATPase beta subunit from a thermophilic Bacillus strain, PS3, was mutagenized to leucine, cysteine or alanine. Each of the mutated beta subunits was isolated and its affinity for ATP-Mg was examined by means of difference circular dichroism and differential titration calorimetry. The Kd values for ATP-Mg obtained were: beta Y341 (wild type), 0.015 mM; beta Y341L, 0.7 mM; beta Y341C and beta Y341A, > 3 mM. All the mutant beta subunits could be reconstituted into the alpha 3 beta 3 gamma complex with alpha and gamma subunits. The alpha 3 beta (mutant)3 gamma complexes hydrolyzed ATP with apparent Vmax values larger than that of the alpha 3 beta (WILD)3 gamma complex. The apparent Km values of the alpha 3 beta (mutant)3 gamma complexes increased in parallel with the Kd values for ATP-Mg of the isolated mutant beta subunits. These results indicate that residue beta Y341 is directly involved in the catalytic ATP-Mg binding and is a major Km-determining residue of F1-ATPase.
Authors:
M Odaka; C Kaibara; T Amano; T Matsui; E Muneyuki; K Ogasahara; K Yutani; M Yoshida
Related Documents :
8243457 - Refined crystal structure of phycoerythrin from porphyridium cruentum at 0.23-nm resolu...
2503507 - Modification of alf-4- and receptor-stimulated phospholipase c activity by g-protein be...
11914377 - Role of the g protein gamma subunit in beta gamma complex modulation of phospholipase c...
9346867 - Spectroscopy and modelling of the cytoplasmic domain of the gamma-subunit of the high a...
8243457 - Refined crystal structure of phycoerythrin from porphyridium cruentum at 0.23-nm resolu...
8953217 - A transferred noe study of a tricyclic analog of acyclovir bound to thymidine kinase.
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  115     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1994 Apr 
Date Detail:
Created Date:  1994-10-18     Completed Date:  1994-10-18     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  789-96     Citation Subset:  IM    
Affiliation:
Chemical Engineering Laboratory, Institute of Physical and Chemical Research, Saitama.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / pharmacology
Amino Acid Sequence
Base Sequence
Binding Sites
Calorimetry / methods
Catalysis
Circular Dichroism
Cysteine / chemistry
Kinetics
Molecular Sequence Data
Mutation
Peptide Fragments / chemistry*
Proton-Translocating ATPases / chemistry*
Thermodynamics
Titrimetry
Tyrosine / chemistry*
Chemical
Reg. No./Substance:
0/Peptide Fragments; 52-90-4/Cysteine; 55520-40-6/Tyrosine; 56-65-5/Adenosine Triphosphate; EC 3.6.3.14/Proton-Translocating ATPases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  The delayed glucocorticoid-responsive and hepatoma cell-selective enhancer of the rat arginase gene ...
Next Document:  Template-dependent peptide formation on ribosomes catalyzed by pyridine.