Carbon dioxide activation of 1-aminocyclopropane-1-carboxylate (ACC) oxidase in ethylene biosynthesis

Poneleit, Loelle; Dilley, David R.

doi:10.1016/0925-5214(93)90055-8

Cited by 30 publications

(8 citation statements)

References 9 publications

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“…Striga germination stimulants, including GR24, were reported to stimulate seed respiration and increase CO 2 concentration by several‐fold ( Brown and Robinson 1949; Vallance 1951a; Logan and Stewart 1995). CO 2 has been shown to be required to make ACCO catalytically competent to produce ethylene ( Poneleit and Dilley 1993; Finlayson and Reid 1994; Mathooko 1996). Results from the present work showed that exogenous CO 2 increased ACCO activity both in intact Striga seeds and in crude enzyme preparations ( Tables 2 and 5).…”

Section: Discussionmentioning

confidence: 99%

Conditioning period, CO₂ and GR24 influence ethylene biosynthesis and germination of Striga hermonthica

Babiker

Sugimoto

et al. 2000

Physiologia Plantarum

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Germination of witchweed (Striga hermonthica [Del.] Benth), an important root parasite on poaceous crops, requires pretreatment ‘conditioning’ in a warm moist environment and a subsequent exposure to a stimulant. The roles of conditioning period, CO2 and a strigol analogue (GR24) in ethylene biosynthesis and germination of the parasite were investigated. Conditioning increased the seeds’ capacity to oxidize exogenous 1‐aminocyclopropane‐1‐carboxylic acid (ACC). Exogenous CO2 increased the seeds capacity to oxidize ACC by 3‐ to 9‐fold. A combination of GR24 and ACC increased ethylene production by more than 3‐fold in comparison with the rates obtained using these compounds separately. Aminoethoxyvinylglycine (AVG) completely inhibited ethylene induction by GR24, but not by ACC. A GR24 treatment, made subsequent to conditioning in GR24, did not induce ethylene. However, seeds conditioned in GR24 and then given 1 mM ACC produced 293 nl l−1 ethylene. ACC oxidase (ACCO) activity in crude extracts was increased by conditioning and CO2. The enzyme displayed an absolute requirement for ascorbate. Absence of exogenous Fe2+ reduced enzyme activity only by 14%. GR24 applied during conditioning reduced germination in response to a subsequent GR24 treatment. ACC was, invariably, less effective in inducing S. hermonthica germination than GR24 even at concentrations which induce more ethylene than concurrent GR24 treatments. The results are consistent with a model in which conditioning removes a restriction on the ethylene biosynthetic pathway in S. hermonthica seeds. GR24 modulates the key enzymes in ethylene biosynthesis. The stimulant suppresses ethylene biosynthesis in unconditioned seeds and promotes it in conditioned ones. Germination of S. hermonthica results from the joint action of GR24 and the ethylene it induces.

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Section: Discussionmentioning

confidence: 99%

Conditioning period, CO₂ and GR24 influence ethylene biosynthesis and germination of Striga hermonthica

Babiker

Sugimoto

et al. 2000

Physiologia Plantarum

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“…The supernatant was used for enzyme assays. The enzyme assay reaction was initiated by combining 600 μL extracted enzyme, 400 μL assay solution containing 0.1 M Tricine (pH 7.5), 10% glycerol, 0.1 mM FeSO 4 , 30 mM ascorbate, 1 mM DTT (Poneleit and Dilley, 1993), and 0.25 mM sodium bicarbonate (Smith and John, 1993), and 1.9 mM ACC. The test tube was then sealed and after incubation with shaking at 25 °C for 20 min, a 1-mL gas sample was withdrawn with a syringe from the headspace for C 2 H 4 determination using the GC described previously.…”

Section: Methodsmentioning

confidence: 99%

Pawpaw [Asimina triloba (L.) Dunal] Fruit Ripening. I. Ethylene Biosynthesis and Production

Koslanund¹,

Archbold²,

Pomper³

2005

jashs

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Pawpaw fruit ethylene production, 1-aminocyclopropane-1-carboxylic acid (ACC) synthase (ACS) and ACC oxidase (ACO) activities, and tissue content of the ethylene precursor ACC and conjugate malonyl-ACC (MACC) were measured during postharvest ripening. Fruit were harvested near the advent of the ripening process and were ripened at room temperature. The fruit displayed increases in ethylene production and respiration rate during ripening with maxima for both 3 days after harvest. Mean ethylene maxima on a fresh weight basis were 4.7 and 7.6 μg·kg-1·h-1 and mean respiratory (CO2 production) maxima on a fresh weight basis were 220 and 239 mg·kg-1·h-1 in 1999 and 2001, respectively. The increase in ethylene evolution coincided with an increase in respiration and a rapid decline in fruit firmness. Internal and external fruit firmness declined in a parallel manner. The ethylene climacteric peak occurred after the greatest decline in fruit firmness, indicating that low levels of ethylene may be sufficient to initiate the ripening process. The ethylene climacteric peak also coincided with the highest activities of both ACS and ACO as well as the maximum tissue ACC content. As ACC content increased, MACC content declined, suggesting a regulation of ethylene production via free ACC levels by malonylation of ACC. Thus, the climacteric development of ethylene production may be regulated by an increase of ACS activity and a decrease in ACC malonyltransferase activity, making more free ACC available for the production of ethylene by increased activity of ACO.

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“…In addition to being related to the 2-oxo acid-dependent dioxygenases by sequence, ACC oxidase resembles them in requiring ferrous iron as a cofactor and dioxygen as a cosubstrate. Unusually ACC oxidase apparently utilizes ascorbate as a co-substrate rather than a 2-oxo acid and CO2 is an activator (Dong et al, 1992a;Fernandez-Maculet et al, 1993;Poneleit and Dilley, 1993;Smith and John, 1993). In vivo mechanistic studies using labelled or modified ACC analogues have demonstrated that the conversion of ACC into ethylene in apple involves a stepwise cleavage of the cylopropane ring of ACC (Adlington et al, 1982;Baldwin et al, 1988); however, little or no in vitro mechanistic or structural studies have been reported.…”

Section: Introductionmentioning

confidence: 99%

Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli

Zhang¹,

Schofield²,

Baldwin³

et al. 1995

Biochemical Journal

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1-Aminocyclopropane-1-carboxylate (ACC) oxidase catalyses the final step in the biosynthesis of the plant hormone ethylene. The successful overexpression and characterization of active ACC oxidase from tomato has been achieved. PCR was used to insert the corrected cDNA coding for the tomato ACC oxidase into the pET-11a expression vector. Cloning of the resultant construct in Escherichia coli BL21(DE3)pLysE gave transformants which expressed ACC oxidase at levels greater than 30% of soluble protein under optimized conditions. When induced by addition of isopropyl-beta-D-thiogalactopyranoside (IPTG) at 37 degrees C the ACC oxidase expressed was less soluble and less active than when induced at 27 degrees C. The enzyme was purified to near homogeneity by a three-step chromatographic procedure. The specific activity of the purified recombinant ACC oxidase was typically 1.3-1.9 mol of ethylene/mol of enzyme per min, higher than values reported for native enzyme. Like the native enzyme it displayed a requirement for ferrous iron and ascorbate, and CO2 was an activator. The ability to discriminate between racemic diastereomers of 1-amino-2-ethyl cyclopropane-1-carboxylic acid was demonstrated. The enzyme was found to have a loose specificity for ascorbate, showing apparent preference for D-ascorbate and 5,6-O-isopropylidene L-ascorbate rather than L-ascorbate. The addition of catalase, dithiothreitol and BSA to incubation mixtures all resulted in significant increases in activity. When treated with diethylpyrocarbonate (DEPC) under mildly acidic conditions, the enzyme rapidly lost activity. Comparison of the rate of inactivation with the increase in absorbance at 240 nm gave results consistent with the modification of two to three histidine residues at the active site, although the possibility of additional modification of other nucleophilic residues cannot be excluded. Inactivation was largely prevented by the addition of substrates and ferrous iron, implying that DEPC treatment results in the modification of active-site histidines, which act as ligands for ferrous iron. CO2 offered no protection against DEPC inactivation, either in the absence or presence of substrates and/or ferrous iron.

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Carbon dioxide activation of 1-aminocyclopropane-1-carboxylate (ACC) oxidase in ethylene biosynthesis

Cited by 30 publications

References 9 publications

Conditioning period, CO₂ and GR24 influence ethylene biosynthesis and germination of Striga hermonthica

Conditioning period, CO₂ and GR24 influence ethylene biosynthesis and germination of Striga hermonthica

Pawpaw [Asimina triloba (L.) Dunal] Fruit Ripening. I. Ethylene Biosynthesis and Production

Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli

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Carbon dioxide activation of 1-aminocyclopropane-1-carboxylate (ACC) oxidase in ethylene biosynthesis

Cited by 30 publications

References 9 publications

Conditioning period, CO2 and GR24 influence ethylene biosynthesis and germination of Striga hermonthica

Conditioning period, CO2 and GR24 influence ethylene biosynthesis and germination of Striga hermonthica

Pawpaw [Asimina triloba (L.) Dunal] Fruit Ripening. I. Ethylene Biosynthesis and Production

Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli

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Conditioning period, CO₂ and GR24 influence ethylene biosynthesis and germination of Striga hermonthica

Conditioning period, CO₂ and GR24 influence ethylene biosynthesis and germination of Striga hermonthica