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Fig. 2 | Biotechnology for Biofuels

Fig. 2

From: Improvement of the catalytic activity and thermostability of a hyperthermostable endoglucanase by optimizing N-glycosylation sites

Fig. 2

Sequence alignment of CTendo45 with other homologous GH45 endoglucanases using Clustal Omega. These enzymes are isolated from Thielavia terrestris (PDB: 5GLY, 64% of sequence identity), Magnaporthiopsis poae ATCC 64411 (KLU88048, 77% of sequence identity), Madurella mycetomatis (KXX82926, 78% of sequence identity), Coniochaeta ligniaria NRRL 30616 (OIW24112, 78% of sequence identity), and Rosellinia necatrix (GAP84246, 72% of sequence identity), respectively. Asterisk indicates the positions which have a single, fully conserved residue. Colon indicates the strongly similar parts among homologous sequences and period means the weakly similar parts among homologous sequences. The potential signal peptide is signed with a black arrow and the V–VI loop is signed with a purple arrow. Conserved and nonconserved asparagine residues in CTendo45 are noted by closed and open inverted triangles, respectively. Highlight blocks specify the catalytic residues Asp32 and Asp144 of CTendo45 in orange. The modifiable and intrinsic N-glycosylation sequences are shaded in yellow and red, respectively. All mutant sites in this study are noted by blue vertical arrows

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