TY - JOUR
T1 - Functionalized bilayer membranes as artificial tryptophan synthase. Characterization of catalytic efficiency, substrate specificity, and reaction selectivity
AU - Murakami, Yukito
AU - Kikuchi, Jun Ichi
AU - Hisaeda, Yoshio
AU - Nakamura, Koichiro
AU - Kitazaki, Tomoyuki
AU - Kaya, Hidenori
N1 - Publisher Copyright:
© 1988 The Chemical Society of Japan.
Copyright:
Copyright 2018 Elsevier B.V., All rights reserved.
PY - 1990/8
Y1 - 1990/8
N2 - Functionalized bilayer membranes having vitamin B6 activity effectively catalyzed β-replacement reactions of serine with indoles to afford the corresponding tryptophan derivatives in aqueous media under mild conditions. Catalytic capability of the present artificial enzyme was subjected to change by changing a combination of molecular components constituting the catalyst system. The structural mode of a hydrophobic pyridoxal derivative as the coenzyme model, the catalytic ability of an amino acid residue placed in a peptide lipid which forms single-walled bilayer vesicles as the apoenzyme model, and the coordination property of added metal ions were found to be responsible for the overall catalytic performance. Multifunctional assistance was observed in the β-replacement reaction of serine with indole, and the reaction proceeded in preference to other side reactions, such as β-elimination, dealdolation, and transamination reactions. Substrate selectivity was found to be primarily dependent on the nucleophilicity of indole derivatives.
AB - Functionalized bilayer membranes having vitamin B6 activity effectively catalyzed β-replacement reactions of serine with indoles to afford the corresponding tryptophan derivatives in aqueous media under mild conditions. Catalytic capability of the present artificial enzyme was subjected to change by changing a combination of molecular components constituting the catalyst system. The structural mode of a hydrophobic pyridoxal derivative as the coenzyme model, the catalytic ability of an amino acid residue placed in a peptide lipid which forms single-walled bilayer vesicles as the apoenzyme model, and the coordination property of added metal ions were found to be responsible for the overall catalytic performance. Multifunctional assistance was observed in the β-replacement reaction of serine with indole, and the reaction proceeded in preference to other side reactions, such as β-elimination, dealdolation, and transamination reactions. Substrate selectivity was found to be primarily dependent on the nucleophilicity of indole derivatives.
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U2 - 10.1246/bcsj.63.2339
DO - 10.1246/bcsj.63.2339
M3 - Article
AN - SCOPUS:0025015599
VL - 63
SP - 2339
EP - 2345
JO - Bulletin of the Chemical Society of Japan
JF - Bulletin of the Chemical Society of Japan
SN - 0009-2673
IS - 8
ER -