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Figure 4 | Malaria Journal

Figure 4

From: Mitochondrial NAD+-dependent malic enzyme from Anopheles stephensi: a possible novel target for malaria mosquito control

Figure 4

Analyses of protein sequence alignments of various MEs. Sequence alignments of maize (NADP+-ME-2, chloroplastic NADP+-ME, and NADP+-ME-4), human (ME-1, ME-2, and ME-3), nematode (NAD+-ME-2), bacterial (NAD+-ME) and A. stephensi ME (mosquito ME). The amino acid sequences of the ME isoforms were analyzed by BLAST against the SwissProt database, and the alignments were generated using CLUSTAL [55]. The amino acid residues highlighted in grey share high homology whereas those in bold are identical. Key amino acids discussed in the text are shown with asterisks, arrows or bars (see text for full description). (A) Sites involved in fumarate activation; (B) Malate binding site; (C) ADP binding site; (D) NAD(P)+ binding domain and sites associated with NAD+ versus NADP+ preference; (E) Other sites also associated with NAD+ versus NADP+ preference. For complete protein nomenclature see Additional file 3.

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