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Figure 4 | BMC Biochemistry

Figure 4

From: Aminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modelling

Figure 4

Multiple alignments of mammalian aminopeptidase B and leukotriene A 4 hydrolase sequences and M1 family signature. Sequences were aligned with ClustalW using the Blosum62 matrix. The multiple alignment of Ap-B (in bold-face) from Rattus norvegicus (RnAp-B; AMPB_RAT), Mus musculus (MmAp-B; NP_663392.1), Homo sapiens (HsAp-B; CAC14047.1) and LTA4H from Rattus norvegicus (RnLTA4H; S20444), Mus musculus (MmLTA4H; JN0066), Homo sapiens (HsLTA4H; NP_000886.1) is shown. Gaps are indicated by dashes. Conserved amino acid positions emanating from the whole M1 family multiple alignments (382 proteins) are shown below the alignment. In this consensus line, amino acids invariant in more than 98% of the sequences (> 377/382) are in bold-face and double underlined, residues conserved in more than 90% of the primary structures (> 343/382) are in bold-face and underlined, those conserved in more than 85% of the sequences (> 324/382) are in bold-face and amino acids conserved in more than 80% of the protein sequences (> 305/382) are shown in normal type. Stars indicate similar residues according to the following rule: T:A:S; I:L:V:M; K:R:H; D:E:Q:N; F:Y; G; P; W; C and are typified according to the percentages described above. Vertical arrows point out the presence of one or several gaps (see the number below or alongside the arrows) just after the indicated amino acid residue in the multiple alignments of 382 sequences.

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