1990
DOI: 10.1016/0378-1119(90)90002-9
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Genomic DNA structure of two new horseradish-peroxidase-encoding genes

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Cited by 56 publications
(21 citation statements)
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“…larities to other plant peroxidase sequences from rice (Reimmann et al, 1992), barley (Thordal-Christensen et al, 1991), wheat (Dudler et al, 1991), Arabidopsis (Intapruk et al, 1991), and horseradish (Fujiyama et al, 1990). Fragments 1 and 3 from PO-C1 are more similar to the amino acid sequences of other plant peroxidases than fragment 2.…”
Section: Purification and Sequence Analysis Of Po-c1mentioning
confidence: 94%
See 1 more Smart Citation
“…larities to other plant peroxidase sequences from rice (Reimmann et al, 1992), barley (Thordal-Christensen et al, 1991), wheat (Dudler et al, 1991), Arabidopsis (Intapruk et al, 1991), and horseradish (Fujiyama et al, 1990). Fragments 1 and 3 from PO-C1 are more similar to the amino acid sequences of other plant peroxidases than fragment 2.…”
Section: Purification and Sequence Analysis Of Po-c1mentioning
confidence: 94%
“…Alignment of amino acid sequences from fragments 1, 2, and 3 of PO-C1 to deduced amino acid sequences of other plant peroxidases. Individual peptides, cleaved from PO-C1 by cyanogen bromide, were sequenced and aligned with deduced sequences of peroxidases from rice (Reimmann et al, 1992), barley (ThordalChristensen et al, 1992), wheat (Dudler et al, 1991), Arabidopsis (Intapruk et al, 1991), and horseradish (Fujiyama et al, 1990). Amino acids sharing identity with the PO-C1 peptides are indicated by dots.…”
Section: Purification and Sequence Analysis Of Po-c1mentioning
confidence: 99%
“…Arabidopsis AP shows significant but relatively low amino acid homology with guaiacol peroxidases of turnip [21], tobacco [18], horseradish [7], etc., except for the N-terminal region (data not shown). The overall homology between AP and guaiacol peroxidases is below 25~o.…”
Section: Amino Acid Sequence Comparisonmentioning
confidence: 99%
“…11,12,24,26]. AP is distinct from another plant peroxidase (guaiacol peroxidase, EC 1.11.1.7), represented by horseradish peroxidase, in the following points: (1) AP shows higher specificity for ascorbate than guaiacol; (2) AP is not a glycoprotein; (3) AP is inactivated under electron donor-depleted conditions; (4) AP has non-haem iron in addition to protohaem; (5) AP is inhibited by thiol reagents; (6) antibody raised against AP does not cross-react with guaiacol peroxidase, and vice versa; (7) neither the amino acid composition nor N-terminal amino acid sequence of AP resembles that of guaiacol peroxidase. While the complete amino acid sequence has been determined for guaiacol peroxidase [41], very little information is available on the primary structure of AP.…”
Section: Introductionmentioning
confidence: 99%
“…However, few reports have described the introduction of peroxidase genes as means to produce insect-and pathogen-resistant plants. The peroxidase gene prxC2 from horseradish encodes a basic peroxidase isoenzyme (Fujiyama et al 1990). Expression of prxC2 is induced by wounding, and the promoter region of prxC2 was therefore used as a model to study the mechanisms of wound-inducible transcription (Kawaoka et al 1994a).…”
mentioning
confidence: 99%