The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.
Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling.
Department of Chemistry, The University of Iowa, Iowa City, IA, USA.
Vanja
V
Stojković
Laura L
LL
Perissinotti
Jeeyeon
J
Lee
Stephen J
SJ
Benkovic
Amnon
A
Kohen
D000409:Alanine / Q000737:chemistry*; D019943:Amino Acid Substitution; D002384:Catalysis; D020134:Catalytic Domain; D004926:Escherichia coli / Q000201:enzymology; D007532:Isoleucine / Q000737:chemistry*; D007700:Kinetics; D056004:Molecular Dynamics Simulation; D009154:Mutation; D009249:NADP / Q000737:chemistry / Q000378:metabolism; D013762:Tetrahydrofolate Dehydrogenase / Q000235:genetics / Q000378:metabolism*
D007532:Isoleucine; D009249:NADP; D013762:Tetrahydrofolate Dehydrogenase; D000409:Alanine