Opportunities and limits in creating new enzymes. Experiences with the NAD-dependent lactate dehydrogenase frameworks of humans and bacteria.
Wilks
H M
HM
Molecular Recognition Center, University of Bristol, School of Medical Sciences, United Kingdom.
Cortes
A
A
Emery
D C
DC
Halsall
D J
DJ
Clarke
A R
AR
Holbrook
J J
JJ
D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D006801:Humans; D007770:L-Lactate Dehydrogenase / Q000737:chemistry*; D008291:Malate Dehydrogenase / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D015202:Protein Engineering / Q000379:methods*; D017434:Protein Structure, Tertiary; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D001426:Bacterial Proteins; D009243:NAD; D009249:NADP; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase