Kinetics of a glycine for Arg-47 human alcohol dehydrogenase mutant can be explained by Lys-228 recruitment into the pyrophosphate binding site

C. L. Stone, Thomas Hurley, L. M. Amzel, M. F. Dunn, W. F. Bosron

Research output: Chapter in Book/Report/Conference proceedingChapter

8 Citations (Scopus)
Original languageEnglish
Title of host publicationAdvances in Experimental Medicine and Biology
Pages429-438
Number of pages10
Volume328
StatePublished - 1993

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Alcohol Dehydrogenase
Diphosphates
Site-Directed Mutagenesis
Liver
NAD
Glycine
Isoenzymes
Lysine
Arginine
Binding Sites
Kinetics
diphosphoric acid
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Stone, C. L., Hurley, T., Amzel, L. M., Dunn, M. F., & Bosron, W. F. (1993). Kinetics of a glycine for Arg-47 human alcohol dehydrogenase mutant can be explained by Lys-228 recruitment into the pyrophosphate binding site. In Advances in Experimental Medicine and Biology (Vol. 328, pp. 429-438)

Kinetics of a glycine for Arg-47 human alcohol dehydrogenase mutant can be explained by Lys-228 recruitment into the pyrophosphate binding site. / Stone, C. L.; Hurley, Thomas; Amzel, L. M.; Dunn, M. F.; Bosron, W. F.

Advances in Experimental Medicine and Biology. Vol. 328 1993. p. 429-438.

Research output: Chapter in Book/Report/Conference proceedingChapter

Stone, CL, Hurley, T, Amzel, LM, Dunn, MF & Bosron, WF 1993, Kinetics of a glycine for Arg-47 human alcohol dehydrogenase mutant can be explained by Lys-228 recruitment into the pyrophosphate binding site. in Advances in Experimental Medicine and Biology. vol. 328, pp. 429-438.
Stone CL, Hurley T, Amzel LM, Dunn MF, Bosron WF. Kinetics of a glycine for Arg-47 human alcohol dehydrogenase mutant can be explained by Lys-228 recruitment into the pyrophosphate binding site. In Advances in Experimental Medicine and Biology. Vol. 328. 1993. p. 429-438
Stone, C. L. ; Hurley, Thomas ; Amzel, L. M. ; Dunn, M. F. ; Bosron, W. F. / Kinetics of a glycine for Arg-47 human alcohol dehydrogenase mutant can be explained by Lys-228 recruitment into the pyrophosphate binding site. Advances in Experimental Medicine and Biology. Vol. 328 1993. pp. 429-438
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