The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy.
1H NMR assignments of the trans and cis isomers of succinyl-Ala-Ala-Pro-Phe-p-nitroanilide were accomplished by two-dimensional NMR techniques. Conformational exchange between the cis and trans isomers was not detected in the two-dimensional exchange spectra (NOESY) until catalytic amounts of FK506-binding protein (FKbp) were added. The addition of FK506 to the enzyme-substrate solution inhibited the enzyme and removed the substrate exchange peaks.
Justice
R M
RM
Lilly Research Laboratories, Eli Lilly and Company Indianapolis, Indiana 46285-0403.
Kline
A D
AD
Sluka
J P
JP
Roeder
W D
WD
Rodgers
G H
GH
Roehm
N
N
Mynderse
J S
JS
D000591:Amino Acid Isomerases / Q000378:metabolism*; D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism; D019696:Peptidylprolyl Isomerase; D011487:Protein Conformation; D011994:Recombinant Proteins; D016559:Tacrolimus
D000900:Anti-Bacterial Agents; D009842:Oligopeptides; D011994:Recombinant Proteins; D000591:Amino Acid Isomerases; D019696:Peptidylprolyl Isomerase; D016559:Tacrolimus