| 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. | |
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MedLine Citation:
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PMID: 8089097 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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M Odaka; C Kaibara; T Amano; T Matsui; E Muneyuki; K Ogasahara; K Yutani; M Yoshida |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of biochemistry Volume: 115 ISSN: 0021-924X ISO Abbreviation: J. Biochem. Publication Date: 1994 Apr |
Date Detail:
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Created Date: 1994-10-18 Completed Date: 1994-10-18 Revised Date: 2007-12-19 |
Medline Journal Info:
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Nlm Unique ID: 0376600 Medline TA: J Biochem Country: JAPAN |
Other Details:
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Languages: eng Pagination: 789-96 Citation Subset: IM |
Affiliation:
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Chemical Engineering Laboratory, Institute of Physical and Chemical Research, Saitama. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphate
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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:
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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
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