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Figure 5
Structure-based alignment of F. nucleatum N-acetylneuraminate lyase (FnNAL) and selected N-acetylneuraminate lyases (NALs) of known structure. (a) The sequence identities to the N-acetylneuraminate lyases from H. influenzae (HiNAL; PDB entry 1f7b; Barbosa et al., 2000BB5), P. multocida (PmNAL; PDB entry 4imd; Huynh et al., 2013BB12), S. aureus (SaNAL; PDB entry 5a8g; Stockwell et al., 2016BB32) and E. coli (EcNAL; PDB entry 1nal; Izard et al., 1994BB13) are 74, 72, 57 and 36%, respectively. The structural alignment was computed using the T-Coffee Expresso server (Armougom et al., 2006BB3) and the figure was produced with ESPript 3 (Robert & Gouet, 2014BB30). Strictly conserved residues across NAL enzymes are shown on a red background. The secondary structure of FnNanA is shown at the top; coils represent helices and arrows represent β-strands. The residues involved in the active site are labelled with small black triangles. (b) Kinetic analysis of F. nucleatum N-acetylneuraminate lyase with Neu5Ac. The data were fitted to the Michaelis–Menten equation with an R2 value of 0.99.

ISSN: 2053-230X
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