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Fig. 1 | Microbial Cell Factories

Fig. 1

From: Identification and immobilization of a novel cold-adapted esterase, and its potential for bioremediation of pyrethroid-contaminated vegetables

Fig. 1

Multiple amino acid sequence alignment of Est684. Multiple alignment of the partial amino acid sequences containing the conserved motifs of G-X-S-X-G and putative catalytic triad residues of alpha/beta hydrolase family proteins. The protein sequences were retrieved from GenBank. The accession numbers of the aligned sequences are for the following organisms: ADC79146, lipase/esterase from uncultured sludge bacterium; AMV32280, acetylxylan esterase precursor from Pirellula sp. SH-Sr6A; AMV38012, acetylxylan esterase precursor from Planctomyces sp. SH-PL62; WP008655619, alpha/beta hydrolase from Rhodopirellula europaea. The alignment was carried out using the Clustal W method. The open boxes indicate amino acid residues belonging to the putative catalytic triad residues, and triangles denote the active site

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