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Biochemical characterization of purified, human recombinant Lys304-->Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme.
Kieweg V, Kräutle FG, Nandy A, Engst S, Vock P, Abdel-Ghany AG, Bross P, Gregersen N, Rasched I, Strauss A, Ghisla S. Kieweg V, et al. Among authors: ghisla s. Eur J Biochem. 1997 Jun 1;246(2):548-56. doi: 10.1111/j.1432-1033.1997.00548.x. Eur J Biochem. 1997. PMID: 9208949 Free article.
Redox properties of human medium-chain acyl-CoA dehydrogenase, modulation by charged active-site amino acid residues.
Mancini-Samuelson GJ, Kieweg V, Sabaj KM, Ghisla S, Stankovich MT. Mancini-Samuelson GJ, et al. Among authors: ghisla s. Biochemistry. 1998 Oct 13;37(41):14605-12. doi: 10.1021/bi981414w. Biochemistry. 1998. PMID: 9772189
., and Liu, H. (1990) Biochemistry 29, 3709-3715], which coincides with a pK increase of Glu376-COOH from approximately 6 to 8-9 [Rudik, I., Ghisla, S., and Thorpe, C. (1998) Biochemistry 37, 8437-8445]. From the pH dependence of the midpoint potentials of hwtMCADH …
., and Liu, H. (1990) Biochemistry 29, 3709-3715], which coincides with a pK increase of Glu376-COOH from approximately 6 to 8-9 [Rudik, I., …
Mechanism of activation of acyl-CoA substrates by medium chain acyl-CoA dehydrogenase: interaction of the thioester carbonyl with the flavin adenine dinucleotide ribityl side chain.
Engst S, Vock P, Wang M, Kim JJ, Ghisla S. Engst S, et al. Among authors: ghisla s. Biochemistry. 1999 Jan 5;38(1):257-67. doi: 10.1021/bi9815041. Biochemistry. 1999. PMID: 9890906
This compares with a decrease of the same pKa to approximately 5 in the complex with unmodified hwtMCADH, which corresponds to a pK shift of approximately 11 pK units, i.e., approximately 65 kJ mol-1 [Vock, P., Engst, S., Eder, M., and Ghisla, S. (1998) Bioch …
This compares with a decrease of the same pKa to approximately 5 in the complex with unmodified hwtMCADH, which corresponds to a pK shift of …
166 results