Sequence analysis of ripening-related cytochrome P-450 cDNAs from avocado fruit.

Bozak, Kristin R.; Yu, Hong; Sirevåg, Reidun; Christoffersen, Rolf E.

doi:10.1073/pnas.87.10.3904

Cited by 122 publications

(77 citation statements)

References 36 publications

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“…The CYPs are a group of redox proteins that catalyze the oxidation steps of various substrates using oxygen and NAD(P)H (Guttikonda et al, 2010;Isin and Guengerich, 2007). The first reported plant CYP gene, CYP71A1, was a ripening-related gene from the mesocarp of an avocado (Bozak et al, 1990). Since its discovery, substantial works have been performed on cloning and characterizing a large array of CYPs.…”

Section: Introductionmentioning

confidence: 99%

The Molecular Cloning and Expression Analysis of a CYP71 Gene in <i> Ginkgo biloba</i> L.

LIU

Cao

Cai

et al. 2016

Not Bot Hort Agrobot Cluj

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Cytochrome P450 monooxygenases (CYPs) are a group of redox proteins that catalyze various oxidative reactions in plant secondary metabolism. To explore the function of the CYP71 gene in Ginkgo biloba under biotic and abiotic stresses, a fulllength CYP gene, designated GbCYP71, was first isolated and characterized from leaves of G. biloba. It contained a 1512-bp open reading frame (ORF) encoding 503 amino-acid-deduced polypeptide whose theoretical molecular weight was 56.9 kDa. The genomic DNA sequence of GbCYP71 contained two exons and one intron. The cDNA of GbCYP71 was subcloned in a pET-32a vector and then transformed into E. coli strain BL21 (DE3). A protein with a molecular weight of 76.4 kDa was subsequently identified and found to be consistent with the above theoretical value. Transient expression analysis revealed that the GbCYP71 protein may be located in the G. biloba cell cytoplasm. GbCYP71 was expressed in almost all ginkgo tissues, including leaves, stamens, gynoecia, stems and, preferentially, roots. Expression-profiling analyses revealed that GbCYP71 can be induced by salinity stress and phytohormone signals, including salicylic acid, abscisic acid, methyl jasmonate and ethephon, but is repressed by heat and cold stresses. These results indicate that GbCYP71 mainly functions in responding to biotic and abiotic stresses.

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Section: Introductionmentioning

confidence: 99%

The Molecular Cloning and Expression Analysis of a CYP71 Gene in <i> Ginkgo biloba</i> L.

LIU

Cao

Cai

et al. 2016

Not Bot Hort Agrobot Cluj

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“…The first plant cytochrome P450 for which the corresponding cDNA was isolated was a ripening-related hemoprotein from the mesocarp of avocado (7,8 (11), the same hydroxylase from mung bean (12), allene oxide synthase from flaxseed (13), and flavonoid 3',5'-hydroxylase from petunia (14). In addition, a cDNA for NADPH-cytochrome P450 reductase has been cloned from mung bean (15).…”

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confidence: 99%

Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C--O phenol-coupling cytochrome P450 from the higher plant Berberis stolonifera.

Kraus¹,

Kutchan²

1995

Proc. Natl. Acad. Sci. U.S.A.

161

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A cDNA encoding a cytochrome P450-dependent oxidase, berbamunine synthase (EC 1.1.3.34; CYP80), from cell suspension cultures of the higher plant Berberis stolonifera Koehne and Wolf (barberry) has been isolated and heterologously expressed in functional form in insect cell culture using a baculovirus-based expression system. This cytochrome P450-dependent enzyme is unusual in that it catalyzes the regio-and stereoselective formation of a C-0 phenol couple in bisbenzylisoquinoline alkaloid biosynthesis without concomitant incorporation of activated oxygen into the product. Consistent with the function of an oxidase rather than a monooxygenase, an essential glycine residue in the distal helix, which forms the oxygen-binding pocket in the well-studied bacterial enzyme P-450cam, is replaced by proline at the equivalent position in berbamunine synthase. This oxidase was accumulated in an active form in insect cell microsomes and accepted electrons from the endogenous NADPH-cytochrome P450 reductase. The heterologously expressed enzyme oxidatively couples either two molecules of (R)-N-methylcoclaurine to form the (R,R) dimer guattegaumerine or one molecule each of (R)-and (S)-Nmethylcoclaurine to form the (R,S) dimer berbamunine. The ratio of the two bisbenzylisoquinolines formed could be altered by reductase source or by varying the enantiomer composition of the substrates.

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“…Cytochrome P-450 from this tissue has been purified and well characterized at the molecular level (DP O'Keefe, KJ Leto [1989] Plant Physiol 89: 1141-1149; KR Bozak, H Yu, R Sirevag, RE Christoffersen [1990] Proc NatI Acad Sci USA 87: 3904-3908). Despite this extensive characterization, the role of the enzyme in vivo was not established.…”

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confidence: 99%

“…However, the natural substrate of the avocado Cyt P-450 was not identified. A ripening-related cDNA from avocado mesocarp has been sequenced that bears significant homology to mammalian Cyt P-450 sequences and codes for an N-terminal amino acid sequence identical to that obtained with purified avocado Cyt P-450 (1).…”

mentioning

confidence: 99%

Interactions of Avocado (Persea americana) Cytochrome P-450 with Monoterpenoids

Hallahan¹,

Nugent²,

Hallahan³

et al. 1992

Plant Physiol.

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The microsomal fraction of avocado (Persea americana) mesocarp is a rich source of cytochrome P-450 active in the demethylation of xenobiotics. Cytochrome P-450 from this tissue has been purified and well characterized at the molecular level (DP O'Keefe, KJ Leto [1989] Plant Physiol 89: 1141-1149; KR Bozak, H Yu, R Sirevag, RE Christoffersen [1990] Proc NatI Acad Sci USA 87: 3904-3908). Despite this extensive characterization, the role of the enzyme in vivo was not established. Optical and electron paramagnetic resonance binding studies described here suggest that the monoterpenoids, nerol and geraniol, are substrates of avocado cytochrome P-450 (spectral dissociation constant of 7.2 and 35 micromolar, respectively). Avocado microsomes have been shown to catalyze the hydroxylation of these monoterpenoids, and both nerol and geraniol have been shown to inhibit the activity of avocado cytochrome P-450 toward the artificial substrate 7-ethoxycoumarin, with nerol a competitive inhibitor of this activity.tides, ofmolecular mass 47 and 48 kD, were isolated. Avocado mesocarp has long been known to be a rich source of Cyt P-450 active in the demethylation of pCMA and other xenobiotics (6,16,28). However, the natural substrate of the avocado Cyt P-450 was not identified. A ripening-related cDNA from avocado mesocarp has been sequenced that bears significant homology to mammalian Cyt P-450 sequences and codes for an N-terminal amino acid sequence identical to that obtained with purified avocado Cyt P-450 (1).Thus, avocado Cyt P-450 is one of the best characterized enzymes of its class in plants. Despite this extensive characterization, the role of the enzyme in vivo remains unclear. In this communication, we present evidence that avocado mesocarp contains Cyt P-450 active in the hydroxylation of the monoterpenoids nerol and geraniol. This activity is well characterized as a Cyt P-450-dependent reaction in the plant Catharanthus roseus (12,14), where the hydroxylation of geraniol initiates the biosynthesis of iridoid monoterpenes and the indole alkaloids.Cyt P-450 enzymes are membrane-associated hemoprotein monooxygenases that are involved in a number of biosynthetic (29) and detoxification (3, 15) pathways in plants. Because of their importance in xenobiotic and drug metabolism, these enzymes have been thoroughly studied in mammalian liver (4), with mechanistic and structural details based to a large extent on studies of the bacterial (Pseudomonas putida) camphor hydroxylase system (23). Although considerable progress has been made in characterizing mammalian and bacterial Cyt P-450 enzymes, much less is known about the plant enzymes. This is due principally to the low amounts of Cyt P-450 present in plant tissues, and the apparent lability of the enzyme following detergent solubilization (7,12,15,25,29).Recently, however, Cyt P-450 active in the demethylation of the artificial substrate (pCMA') was purified from avocado mesocarp tissue (16). Two immunologically similar polypep-'Abbreviations: pCMA, 4-chloro-N-me...

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Sequence analysis of ripening-related cytochrome P-450 cDNAs from avocado fruit.

Abstract: The ripening of avocado fruit is associated with the expression of a number of mRNAs concomitant with overt changes in texture and flavor. Two overlapping cDNAs for a mRNA that accumulates during ripening were identified.

Cited by 122 publications

References 36 publications

The Molecular Cloning and Expression Analysis of a CYP71 Gene in <i> Ginkgo biloba</i> L.

The Molecular Cloning and Expression Analysis of a CYP71 Gene in <i> Ginkgo biloba</i> L.

Molecular cloning and heterologous expression of a cDNA encoding berbamunine synthase, a C--O phenol-coupling cytochrome P450 from the higher plant Berberis stolonifera.

Interactions of Avocado (Persea americana) Cytochrome P-450 with Monoterpenoids

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