Skip to main content
Fig. 2 | BMC Biotechnology

Fig. 2

From: A novel eurythermic and thermostale lipase LipM from Pseudomonas moraviensis M9 and its application in the partial hydrolysis of algal oil

Fig. 2

Multiple sequence alignment. a Multiple sequence alignment between LipM and other closely family I.3 Lipases: AHB29478, LipM from Pseudomonas moraviensis M9; 2z8x, PML from Pseudomonas sp. MIS38; WP_010460388, LipT from Pseudomonas mandelii JR-1; AAP76488 and AAP76489, LipA and LipB from uncultured bacterium; ABY86751, lip35 from Pseudomonas sp. lip35; AFP20145, Lip I.3 from Pseudomonas sp. CR-611. Empty triangles () represent putative catalytic residues at the corresponding positions of Ser153, Asp202 and His260. Sequence alignment was performed with Cluster 1.83 and visualized using ESpript 2.2. The alpha helix, beta sheet, random coil and beta turn are identical to α, β, η and T, respectively. 1: T5 primer; 2: T3 primer; 3: conserved catalytic motif; 4-5: the repetitive nine-residue motif GGXGXDXUX; 6: 18-residue amphipathic α-helix; 7: hydrophobic five-residue conserved motif; 8: four hydrophobic residues

Back to article page