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
CL
Department of Biochemistry and Molecular Biology, and Medicine Indiana University School of Medicine, Indianapolis 46202.
Hurley
T D
TD
Amzel
L M
LM
Dunn
M F
MF
Bosron
W F
WF
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D001120:Arginine / Q000737:chemistry / Q000235:genetics; D001665:Binding Sites; D011756:Diphosphates / Q000378:metabolism*; D005998:Glycine / Q000737:chemistry / Q000235:genetics; D006801:Humans; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008239:Lysine / Q000737:chemistry; D016297:Mutagenesis, Site-Directed; D009243:NAD / Q000378:metabolism
D011756:Diphosphates; D007527:Isoenzymes; D009243:NAD; D001120:Arginine; D000426:Alcohol Dehydrogenase; D008239:Lysine; D005998:Glycine