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Fig. 2 | Microbial Cell Factories

Fig. 2

From: Two novel deep-sea sediment metagenome-derived esterases: residue 199 is the determinant of substrate specificity and preference

Fig. 2

Amino acid sequence alignment of DMWf18-543- and DMWf18-558-related lipolytic enzymes. The accession numbers of the enzymes in the GenBank database are given for DMWf18-543 and DMWf18-558 (from this study), Est6 (AFB82690), Est4 (AFB82689), EstMY (ADM67447), and ArmEst1 (AGF91877). Sequence alignment was performed using the ClustalX and ESPript programs. Identical and similar residues among groups are indicated in white text on a red background and in red text on a white background, respectively. Solid circles indicate the locations of the residues involved in the oxyanion hole (glycine (G)). The triangles indicate the locations of the catalytic active site residues (serine (S), aspartate (D), and histidine (H)). The square indicates the location of residue Leu199 of DMWf18-543 and residue Ala199 of DMWf18-558. The conserved HGGG and GXSXG motifs, in which the oxyanion hole and catalytic triad are located, are outlined with boxes

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