Identification and Functional Analyses of Two cDNAs That Encode Fatty Acid 9-/13-Hydroperoxide Lyase (CYP74C) in Rice

Kuroda, Hisao; Oshima, Toshiyuki; Kaneda, Hirotaka; Takashio, Masachika

doi:10.1271/bbb.69.1545

Cited by 36 publications

(30 citation statements)

References 23 publications

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“…These data in agreement with those previously published (Kuroda et al, 2005), clearly show that OsHPL1 and OsHPL2 metabolize 13-HPOT/D and 9-HPOT/D equally well with no apparent substrate preference. In contrast, OsHPL3 is exclusively active on 13-HPOT (Fig.…”

Section: Substrate Preference Of Recombinant Oshpls Matches Their Physupporting

confidence: 93%

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Rice HYDROPEROXIDE LYASES with Unique Expression Patterns Generate Distinct Aldehyde Signatures in Arabidopsis

et al. 2006

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HYDROPEROXIDE LYASE (HPL) genes encode enzymes that catalyze the cleavage of fatty acid hydroperoxides into aldehydes and oxoacids. There are three HPLs in rice (Oryza sativa), designated OsHPL1 through OsHPL3. To explore the possibility of differential functional activities among these genes, we have examined their expression patterns and biochemical properties of their encoded products. Transcript analysis indicates that these genes have distinct patterns and levels of expression. OsHPL1 is ubiquitously expressed, OsHPL2 is expressed in the leaves and leaf sheaths, whereas OsHPL3 is wound inducible and expressed exclusively in leaves. OsHPLs also differ in their substrate preference as determined by in vitro enzyme assays using 9-/13-hydroperoxy linolenic and 9-/13-hydroperoxy linoleic acids as substrates. OsHPL1 and OsHPL2 metabolize 9-/13-hydroperoxides, whereas OsHPL3 metabolizes 13-hydroperoxy linolenic acid exclusively. Sequence alignments of the HPL enzymes have identified signature residues potentially responsible for the substrate specificity/preference of these enzymes. All three OsHPLs are chloroplast localized as determined by chloroplast import assays and green fluorescent protein (GFP) fusion studies. Aldehyde measurements in transgenic Arabidopsis (Arabidopsis thaliana) plants overexpressing individual OsHPL-GFP fusions indicate that all rice HPLs are functional in a heterologous system, and each of them generates a distinct signature of the metabolites. Interestingly, these aldehydes were only detectable in leaves, but not in roots, despite similar levels of OsHPL-GFP proteins in both tissues. Similarly, there were undetectable levels of aldehydes in rice roots, in spite of the presence of OsHPL1 transcripts. Together, these data suggest that additional tissue-specific mechanism(s) beyond transcript and HPL enzyme abundance, regulate the levels of HPL-derived metabolites.

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Section: Substrate Preference Of Recombinant Oshpls Matches Their Physupporting

confidence: 93%

“…The existence of two of these genes (OsHPL1 and 2) was recently reported (Kuroda et al, 2005). These authors, however, restricted their investigation to the in vitro activity assays of the encoded products and classified both enzymes as 9-/13-HPLs.…”

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confidence: 99%

Rice HYDROPEROXIDE LYASES with Unique Expression Patterns Generate Distinct Aldehyde Signatures in Arabidopsis

et al. 2006

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“…This indicated that the purified recombinant HPL could be used to produce volatile aldehydes, which are widely used in food industries and cosmetic industries. As reported, HPL cleaves 13-HPOT to (3Z)-hexenal, but (3Z)-hexenal was enzymatically or spontaneously isomerized into more stable 2(E)-hexenal [6,20].…”

Section: Enzyme Activity and Product Identificationsupporting

confidence: 53%

“…9-/13-HPL cleaves 9-HPOT and 9-HPOD into 3(Z)-nonadienal and 3(Z)-nonenal, respectively. 3(Z)-hexenal, 3(Z)-nonadienal, and 3(Z)-nonenal are enzymatically or spontaneously isomerized into more stable 2(E)-hexenal, 2(E)-nonadienal, and 2(E)-nonenal [6]. It has been revealed that HPL from potato leaves only has 13-HPL activity [7].…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning, expression, and enzymatic characterization of Solanum tuberosum hydroperoxide lyase

Xue

Jiang

et al. 2012

Eur Food Res Technol

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A cDNA encoding hydroperoxide lyase (HPL) was isolated from Solanum tuberosum, cloned into pQE-30 vector, and expressed in E. coli. The recombinant protein was purified by nickel affinity chromatography and showed an approximate molecular weight of 54 kDa by SDS-PAGE analysis, which was similar to the predicted value based on the putative amino acid sequences (53.9 kDa). 13-Hydroperoxy-linolenic acid (13-HPOT) was the preferred substrate for the enzyme compared with 13-hydroperoxy-linoleic acid (13-HPOD). The corresponding volatile products were 2(E)-hexenal and n-hexanal tested by headspace-gas chromatography, respectively. The enzyme was optimally active at 25°C and pH 6.5. The K m , V max , and the catalytic efficiency (V max /K m ) for 13-HPOT were 56.6 lM, 71.3 units/mg, and 1.26 units/mg Á lM, respectively. Activity of the recombinant potato HPL increased when Triton X-100, sodium chloride, or potassium chloride was added in the reaction mixture, while calcium chloride decreased activity of the recombinant enzyme.

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“…Hydroperoxide lyase activities, functionally assigned to the CYP74B subfamily in Arabidopsis [15] and Medicago sativa (alfalfa) [16], have also been demonstrated for the more distantly related CYP74E and CYP74F subfamilies in rice (CYP74E2/OsHPL1, CYP74E1/OsHPL2 and CYP74F1/OsHPL3) [17,18]. These activities have also been assigned to moss CYP74G1 (AJ316567) [19] and claimed for Z. mays CYP74F2 (AY540745, US patent 51 71 72 73 74 75 76 77 78 51 clan 71 clan 79 80 81 82 83 84 89 92 93 98 99 701 703 705 706 712 72 clan 74 clan 709 714 715 721 719 723 726 736 734 735 [134,135], with the placement of Vitis based on the chloroplast phylogeny of Jansen et al, 2006 [131].…”

Section: Introductionmentioning

confidence: 92%

Comparison of Cytochrome P450 Genes from Six Plant Genomes

Nelson

Ming

Alam

et al. 2008

Tropical Plant Biol.

132

127

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Plants depend on cytochrome P450 (CYP) enzymes for nearly every aspect of their biology. In several sequenced angiosperms, CYP genes constitute up to 1% of the protein coding genes. The angiosperm sequence diversity is encapsulated by 59 CYP families, of which 52 families form a widely distributed core set. In the 20 years since the first plant P450 was sequenced, 3,387 P450 sequences have been identified and annotated in plant databases. As no new angiosperm CYP families have been discovered since 2004, it is now apparent that the sampling of CYP diversity is beginning to plateau. This review presents a comparison of 1,415 cytochrome P450 sequences from the six sequenced genomes of Vitis vinifera (grape), Carica papaya (papaya), Populus trichocarpa (poplar), Oryza sativa (rice), Arabidopsis thaliana (Arabidopsis or mouse ear's cress) and Physcomitrella patens (moss). An evolutionary analysis is presented that tracks land plant P450 innovation over time from the most ancient and conserved sequences to the newest dicot-specific families. The earliest or oldest P450 families are devoted to the essential biochemistries of sterol and carotenoid synthesis. The next evolutionary radiation of P450 families appears to mediate crucial adaptations to a land environment. And, the newest CYP families appear to have driven the diversity of angiosperms in mediating the synthesis of pigments, odorants, flavors and order-/genus-specific secondary metabolites. Family-by-family comparisons allow the visualization of plant genome plasticity by whole genome duplications and massive gene family expansions via tandem duplications. Molecular evidence of human domestication is quite apparent in the repeated P450 gene duplications occurring in the grape genome.

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Identification and Functional Analyses of Two cDNAs That Encode Fatty Acid 9-/13-Hydroperoxide Lyase (CYP74C) in Rice

Cited by 36 publications

References 23 publications

Rice HYDROPEROXIDE LYASES with Unique Expression Patterns Generate Distinct Aldehyde Signatures in Arabidopsis

Rice HYDROPEROXIDE LYASES with Unique Expression Patterns Generate Distinct Aldehyde Signatures in Arabidopsis

Molecular cloning, expression, and enzymatic characterization of Solanum tuberosum hydroperoxide lyase

Comparison of Cytochrome P450 Genes from Six Plant Genomes

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