Conformations of bound nucleoside triphosphate effectors in aspartate transcarbamylase. Evidence for the London-Schmidt model by transferred nuclear Overhauser effects

Transferred nuclear Overhauser effects were used to determine the conformations of ATP, CTP, and ITP bound to the regulatory site of aspartate transcarbamylase. The results are in accord with the predictions of the London-Schmidt model [London, R. E., & Schmidt, P. G. (1972) Biochemistry 11, 313...

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Published inBiochemistry (Easton) Vol. 24; no. 7; pp. 1593 - 1598
Main Authors Banerjee, Anirban, Levy, H. Richard, Levy, George C, Chan, William W. C
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 01.03.1985
Subjects
Allosteric Site
Aspartate Carbamoyltransferase - metabolism
Biological and medical sciences
Enzyme Activation - drug effects
Fundamental and applied biological sciences. Psychology
Interactions. Associations
Intermolecular phenomena
Magnetic Resonance Spectroscopy
Models, Chemical
Molecular biophysics
Molecular Conformation
Ribonucleotides - metabolism
Ribonucleotides - pharmacology
Enzyme
Aspartate carbamoyltransferase
Overhauser effect
Molecular interaction
NMR spectrometry
ATP
Conformation induction
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Summary:Transferred nuclear Overhauser effects were used to determine the conformations of ATP, CTP, and ITP bound to the regulatory site of aspartate transcarbamylase. The results are in accord with the predictions of the London-Schmidt model [London, R. E., & Schmidt, P. G. (1972) Biochemistry 11, 3136] and show that ATP and CTP bind in the anti conformation while ITP binds in the syn conformation.
Bibliography:ark:/67375/TPS-WGFTQFQJ-P
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ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00328a003