Alpha/beta hydrolases

Ollis, D.L., Cheah, E., Cygler, M. etal. (1970) The alpha/beta hydrolase fold. Protein Engineering, 5, 197-211. 

Holmquist, M. (2000) Alpha/beta-hydrolase fold enzymes structures, functions and mechanisms. Current Protein Peptide Science, 1, 209-235. 

Andexer, J., von Langermann, J., Mell, A. et al. (2007) An R-selective hydroxynitrile lyase from Arabidopsis thaliana with an alpha/beta-hydrolase fold. Angewandte Chemie-International Edition, 46, 8679-8681. 

Hisano, T., Hata, Y., Fujii, T., Liu, J. Q., Kurihara, T., Esaki, N., and Soda, K. (1996). Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/ beta hydrolase structure that is different from the alpha/beta hydrolase fold./ Biol. Chem. 271, 20322-20330. 

The lipid messenger OEA links dietary fat intake to satiety. CellMetab. 8, 281-288. Simon, G. M., and Cravatt, B. F. (2006). Endocannabinoid biosynthesis proceeding through glycer-ophospho-jV-acyl ethanolamine and a role for alpha /beta-hydrolase 4 in this pathway. J. Biol. 

Nardini M, Dijkstra BW. Alpha/beta hydrolase fold enzymes the family keeps growing. Curr. Opin. Struct. Biol. 1999 9 732-737. 

Hotelier T, Renault L, Cousin X, Negre V, Marchot P, Chaton-net A. ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins. Nucleic Acids Res. 2004 32 D145-147. 

Chatonnet, A., Hotelier, T., and Cousin, X. 1999. Kinetic parameters of cholinesterase interactions with organophosphates retrieval and comparison tools available through ESTHER database ESTerases, alpha/beta hydrolase enzymes and relatives. Chem.-Biol. Interact., 119/120, 567-576. 

Skjot, M., De Maria, L., Chatterjee, R., Svendsen, A., Patkar, S.A., 0stergaard, P.R.,and Brask,). (2009) Understanding the plasticity of the alpha/beta-hydrolase fold lid swapping on the Candida antarctica lipase B results in chimeras with interesting biocatalytic properties. ChemBioChem., 10,520-527. 

For the malonate group to be used for fatty acid synthesis, it must first be transferred from malonyl-CoA to malonyl-ACP by the 32.4-kDa monomeric malonyl-CoA ACP transacy-lase, the product of the fabD gene (Fig. 2). A stable malonyl-serine enzyme intermediate is formed during the course of the FabD reaction, and subsequent nucleophilic attack on this ester by the sulfhydryl of ACP yields malonyl-ACP. The high reactivity of the serine in malonyl-ACP transacylase is due to the active site being composed of a nucleophilic elbow as observed in alpha/beta hydrolases. The serine is hydrogen bonded to His-201 in a fashion similar to serine hydrolases. 

Holmquist, M. 2000. Alpha Beta-Hydrolase Fold Enzymes Structures, Functions and Mechanisms. Current Protein Peptide Science 1 (2) 209-235. 

A. (1992). The Alpha/Beta - Hydrolase Fold. Protein Engineering,design selectiom Vol. 5, No.3 pp. 197-211... 

Van PouderoyenG, E ertT, Jaeger KE, Dijkstra BW (2001) The crystal structure of Bacillus subtilis lipase a minimal alpha/beta hydrolase fold enzyme. J Mol... 

Lazniewski M, Steczkiewicz K, Knizewski L, Wawer I, Ginalski K (2011) Novel transmembrane lipases of alpha/beta hydrolase fold. FEES Lett 585 870-874... 

ESTHER ESTerases and alpha/beta Hydrolase Enzymes and Relatives databa.se... 

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