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. 1999 Jun;120(2):501–512. doi: 10.1104/pp.120.2.501

Figure 1.

Figure 1

Amino acid sequence of Prx7 and alignment to selected peroxidases. Alignment to peroxidases from barley: Prx8 (pBH6-301; Thordal-Christensen et al., 1992), BP1 (Rasmussen et al., 1991b), and horseradish HRP-C gene A (Welinder, 1979; Fujiyama et al., 1988). The lower line shows invariant residues, and variable residues are indicated by dots. The eight Cys residues forming disulfide bridges and the two His residues essential for catalysis are indicated in bold and are underlined. Gaps (-) are introduced to maximize the alignment. N- and C-terminal sequences shown to be absent from the mature proteins are in lowercase italics. Residues shown in bold in Prx7 were determined by amino acid sequencing. Underlined regions in the Prx7 sequence correspond to peptides identified by MALDI-TOF MS tryptic fingerprinting. The underlined and bold Asn residues at positions 91 and 176 in the Prx7 sequence are putative N-glycosylation sites.