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Aspartate transcarbamoylase transition

E.R. Kantrowitz and W.N. Lipscomb. 1990. Escherichia coli aspartate transcarbamoylase The molecular basis for a concerted allosteric transition Trends Biochem. Sci. 15 53-59. (PubMed)... [Pg.450]

H.K. Schachman. 1988. Can a simple model account for the allosteric transition of aspartate transcarbamoylase J. Biol. Chem. 263 18583-18586. (PubMed)... [Pg.450]

W.E. Werner and H.K. Schachman. 1989. Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments J. Mol. Biol. 206 221-230. (PubMedl... [Pg.451]

Figure 10.9 The T-to-R state transition in ATCase. Aspartate transcarbamoylase exists in two conformations a compact, relatively inactive form called the tense (T) state and an expanded form called the relaxed (R) state. Notice that the structure of ATCase changes dramatically in the tramsition from the T state to the R State. PALA binding stabilizes the R state. Figure 10.9 The T-to-R state transition in ATCase. Aspartate transcarbamoylase exists in two conformations a compact, relatively inactive form called the tense (T) state and an expanded form called the relaxed (R) state. Notice that the structure of ATCase changes dramatically in the tramsition from the T state to the R State. PALA binding stabilizes the R state.
AtTfiyfv profile. A histidine residue in the active site of aspartate transcarbamoylase is thought to be important in stabilizing the transition state of the bound substrates. Predict the pH dependence of the catalytic rate, assuming that this interaction is essennal and dominates the pH-aclivity profile of the enzyme, (Seeeciuations on p. lb.)... [Pg.299]

See other pages where Aspartate transcarbamoylase transition is mentioned: [Pg.191]    [Pg.143]    [Pg.442]    [Pg.297]    [Pg.298]    [Pg.300]    [Pg.290]   
See also in sourсe #XX -- [ Pg.54 , Pg.55 ]



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Aspartate transcarbamoylase

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