Abstract
The S1′ substrate specificity of the sunflower seed major aminopeptidase was studied with a series of dipeptide substrates with phenylalanine at P1 and a hydrophobic amino acid at P1′ position. The kinetic parameters of hydrolysis are significantly affected by the structure, side chain hydrophobicity and configuration of the P1′ moiety. Its binding during enzyme-substrate complex formation takes place at a hydrophobic site of limited size following an extraction mechanism as seen from the applied structure-activity correlation. Attempts to establish such dependencies for the catalytic step of the reaction reveal the presence of additional S1′-P1′ enzyme-substrate interactions of greater complexity.
References
Tishinov K, Stambolieva N, Petrova S, Galunsky B, Nedkov P, Acta Physiol Plant, 31 (2009) 199.
Denton P, Bioorg Chem, 28 (2000) 205.
Dorovska VN, Varfolomeyev SD, Kazanskaya NF, Klyosov AA, Martinek K, FEBS Lett, 23 (1972) 122.
Jarv J, Kesvatera T, Aaviksaar A, Eur J Biochem, 67 (1976) 315.
Jarv J & Ragnarsson U, Bioorg Chem, 19 (1991) 77.
Gagnon P, Huang X, Therrien E, Keillor JW, Tetrahedron Lett, 43 (2002) 7717.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Tishinov, K., Stambolieva, N., Nedkov, P. et al. Sunflower Seed Aminopeptidase-Catalyzed Hydrolysis of Phe-Xaa Dipeptides — Exploring the S1′ Specificity of the Enzyme. J. Plant Biochem. Biotechnol. 18, 237–239 (2009). https://doi.org/10.1007/BF03263327
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF03263327