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Segel, I. H. Enzyme Kinetics; John Wiley and Sons: New York, 1993; pp 170-178.
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Segel, I.H.1
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+2 was assigned a charge of +2. The minimization involved Phe, 2 and residues within a 15 A radius around the active site and was conducted until the energy difference between iterations was less than 1 cal/mol.
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84986870156
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+2 was assigned a charge of +2. The minimization involved Phe, 2 and residues within a 15 A radius around the active site and was conducted until the energy difference between iterations was less than 1 cal/mol.
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Expression 1.0 was derived using the King-Altman method: King, E. L.; Altman, C. J. J. Phys. Chem. 1956, 60, 1375.
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0342999655
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note
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Kinetic data were analyzed using the software package Grafit 3.01® (©Erithacus Software Ltd.)
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22
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0022503728
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Hydrolysis, rather than product release, is the rate-limiting step for the peptidase activity of CPA: (a) Galdes, A.; Auld, D. S.; Vallee, B. L. Biochemistry 1986, 25, 646;
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Auld, D.S.5
Vallee, B.L.6
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24
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0002714948
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2+ (where His-69, Glu-72 and His-196 are the other active site ligands): (a) Lipscomb, W. N. Acc. Chem. Res. 1970, 3, 81;
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Lipscomb, W.N.1
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27
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0342602813
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Chapman and Hall: New York, Molecular modeling with the ionized form of 2 yielded a structure qualitatively very similar to the complex of non-ionized 2 with CPA which is described above
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a was determined spectrophotometrically (Albert, A; Sargeant, E. P. The Determination of Ionization Constants, 3rd ed; Chapman and Hall: New York, 1984; pp 70-101). Molecular modeling with the ionized form of 2 yielded a structure qualitatively very similar to the complex of non-ionized 2 with CPA which is described above.
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The Determination of Ionization Constants, 3rd Ed
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Albert, A.1
Sargeant, E.P.2
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