[Peptide synthesis catalyzed by subtilisin-72 in organic solvents].
The solubility, stability, and activity of native subtilisin 72 and of its complex with SDS were comparatively studied in a number of polar organic solvents. Subtilisin was found to catalyze peptide bond formation when suspended in acetonitrile or solubilized as a complex with SDS in ethanol and isopropanol. Tripeptide Z-Ala-Ala-Leu-pNA, tetrapeptides A-Ala-Ala-P1-P1'-B, where A = Z or Abz; P1 = Leu, Phe, Met, Trp, Ile, Tyr, Phe(NO2), or Glu(OMe), P1' = Leu, Phe, Glu, Ala, Ile, Val, or Arg; B = NH2, pNA, or 2-(2,4-dinitrophenyl)aminoethylamine residue (Ded); pentapeptides Z-Ala-Ala-Leu-Ala-Ala-pNA and Z-Ala-Ala-Leu-Ala-Phe-pNA; and hexapeptide Abz-Val-Ala-Phe-Phe-Ala-Ala-Ded were synthesized using the SDS-subtilisin complex. The complex also efficiently catalyzed the oligomerization of tripeptide H-Phe-Ala-Leu-OCH3 in ethanol, which resulted in a 63:37 mixture of trioligomer and tetraoligomer. It was demonstrated that SDS-subtilisin is a much more efficient catalyst than the suspension of native enzyme.
Getun
I V
IV
Faculty of Chemistry, Moscow State University, Russia.
Filippova
I Iu
IIu
Lysogorskaia
E N
EN
Bacheva
A V
AV
Oksenoĭt
E S
ES
D002384:Catalysis; D004795:Enzyme Stability; D010455:Peptides / Q000138:chemical synthesis*; D012997:Solvents; D013381:Subtilisins / Q000378:metabolism*
D010455:Peptides; D012997:Solvents; D013381:Subtilisins
Peptidnyĭ sintez, kataliziruemyĭ subtilizinom-72 v organicheskikh rastvoriteliakh.