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SHR Neuro Cancer Cardio Lipid Metab Microb

Perz, V; Baumschlager, A; Bleymaier, K; Zitzenbacher, S; Hromic, A; Steinkellner, G; Pairitsch, A; Łyskowski, A; Gruber, K; Sinkel, C; Küper, U; Ribitsch, D; Guebitz, GM.
Hydrolysis of synthetic polyesters by Clostridium botulinum esterases.
Biotechnol Bioeng. 2016; 113(5): 1024-1034. Doi: 10.1002/bit.25874
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Leading authors Med Uni Graz: Perz Veronika
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Abstract:: Two novel esterases from the anaerobe Clostridium botulinum ATCC 3502 (Cbotu_EstA and Cbotu_EstB) were expressed in Escherichia coli BL21-Gold(DE3) and were found to hydrolyze the polyester poly(butylene adipate-co-butylene terephthalate) (PBAT). The active site residues (triad Ser, Asp, His) are present in both enzymes at the same location only with some amino acid variations near the active site at the surrounding of aspartate. Yet, Cbotu_EstA showed higher kcat values on para-nitrophenyl butyrate and para-nitrophenyl acetate and was considerably more active (sixfold) on PBAT. The entrance to the active site of the modeled Cbotu_EstB appears more narrowed compared to the crystal structure of Cbotu_EstA and the N-terminus is shorter which could explain its lower activity on PBAT. The Cbotu_EstA crystal structure consists of two regions that may act as movable cap domains and a zinc metal binding site. © 2015 Wiley Periodicals, Inc.
Find related publications in this database (using NLM MeSH Indexing): Butyrates - metabolism; Catalytic Domain -; Clostridium botulinum - chemistry; Clostridium botulinum - enzymology; Clostridium botulinum - metabolism; Crystallography, X-Ray -; Esterases - chemistry; Esterases - metabolism; Hydrolysis -; Models, Molecular -; Nitrophenols - metabolism; Polyesters - metabolism; Protein Conformation -; Substrate Specificity -; Zinc - metabolism
Find related publications in this database (Keywords): polyesterase; esterase; polymer hydrolysis; anaerobic digestion; zinc dependent enzyme; (poly(butylene adipate-co-butylene terephthalate) (PBAT)