Inhibition of glycollate oxidase from pea leaves

Jewess, P. J.; Kerr, M. W.; Whitaker, D P

doi:10.1016/0014-5793(75)80039-1

Cited by 49 publications

(15 citation statements)

References 12 publications

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“…L-MSO is a well known inhibitor of glutamine synthetase (17) and AAN, an analog of glycine, has been reported to inhibit glycine decarboxylase (8). AOA is known to block principally serine:glyoxylate aminotransferase (1 1) and BHB to inhibit glycolate oxidase (12). Inhibition of photosynthesis in presence of BHB probably indicates that either nonmetabolized phosphoglycolate or glycolate is toxic for this metabolism.…”

Section: Discussionmentioning

confidence: 99%

Photorespiratory Properties of Mesophyll Protoplasts of Nicotiana plumbaginifolia

Rey¹,

Peltier²

1989

Plant Physiol.

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The photorespiratory activity of mesophyll protoplasts of Nicotlana plumbaglnhfolla has been clearly demonstrated by the presence of a Warburg-effect, the occurrence of an important C02-sensitive 02 uptake and the effect of some photorespiratory inhibitors on photosynthetic activity. At a nonsaturating dissolved inorganic carbon (DIC) concentration (0.1 millimolar), we observed that the rate of CO2 fixation was 60% lower at 50% 02 compared to that measured at 2% 02. Using 1802 and mass spectrometry, we measured 02 exchange as a function of light intensity and of DIC concentration. Oxygen uptake measured at the CO2 compensation point (47.4 micromoles 02 per hour per milligram chlorophyll) was three-fold higher than that measured at a saturating CO2 concentration. Cyanide or iodoacetamide, inhibitors of the Calvin cycle, were found to reduce the 02 uptake to the same extent as CO2 saturation. We conclude from these results that the major part of the C02-sensitive 02 uptake is due to photorespiration. Further, we investigated the effect on net photosynthesis of some inhibitors of the glycolate pathway. At CO2 saturation (10 millimolar DIC), 5 millimolar aminoacetonitrile (AAN), and I millimolar aminooxyacetate (AOA) did not cause any significant decrease in net photosynthesis. However, when these two inhibitors were added under a period of active photorespiration (10 minutes at the CO2 compensation point at 20% 02), we observed a decrease in the rate of net photosynthesis at 10 millimolar DIC measured afterward (respectively, 18 and 29%).This inhibition did not appear at 2% 02, but was stronger at 50% 02 (40% for AAN and 47% for AOA). With 0.05 millimolar butyl 2-hydroxy-3-butynoate (BHB) or 0.5 millimolar L-methionine-DL-sulfoximine (L-MSO), rates of net photosynthesis at 10 millimolar DIC were decreased by 10 to 15%. Additional decreases were observed after a period at the CO2 compensation point at 20% 02 (30% for BHB and 20% for L-MSO). From the sites of action of the four inhibitors tested, we suggest the inhibition of photosynthesis occurring after a period of active photorespiration to be due to the toxic accumulation of nonmetabolized phosphoglycolate. tion between 02 and CO2 at the active site of Rubisco,' the enzyme catalyzing the initial reactions ofboth photosynthetic and photorespiratory metabolisms. In other experiments, the activity of the photosynthetic carbon oxidation cycle was deduced from the effect on photosynthesis of some photorespiratory inhibitors. AAN, an inhibitor of the conversion of glycine to serine, has been shown to cause a decrease in the photosynthetic activity in protoplasts of Triticum aestivum (29), only when added in conditions of active photorespiration. Such an inhibition is usually attributed to the accumulation of nonmetabolized photorespiratory intermediates. According to Servaites and Ogren (27), the inhibition of photosynthesis would result from a deficiency in the recycling of carbon in the Calvin cycle, but Creach and Stewart (5) did not observe a decrease in th...

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Section: Discussionmentioning

confidence: 99%

Photorespiratory Properties of Mesophyll Protoplasts of Nicotiana plumbaginifolia

Rey¹,

Peltier²

1989

Plant Physiol.

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“…modification of the bound F M N (Walsh et al, 1972a). This observation is universal for all the flavin-dependent a-hydroxy acid oxidizing enzymes subsequently examined, including the membraneous D-lactate and L-lactate dehydrogenases of Escherichia coli (Walsh et al, 1972b), the L-hydroxy acid oxidase from rat kidney (Cromartie and Walsh, 1975a,b), the yeast hemeflavoprotein cytochrome b2 (Lederer, 1974), and spinach glycolate oxidase (Jewess et al, 1975). Model studies from Hemmerich's laboratory (Zeller et al, 1972;Gartner, 1974) have shown that photoaddition of dimethylpropargylamine and flavins yields covalent adducts with structures similar to those found in the enzymatic experiments.…”

mentioning

confidence: 85%

Kinetic studies on the inactivation of L-lactate oxidase by [the acetylenic suicide substrate]2-hydroxy-3-butynoate

Ghisla¹,

Ogata²,

Massey³

et al. 1976

Biochemistry

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2-Hydroxy-3-butynoate is both a substrate and an irreversible inactivator of the flavoenzyme L-lactate oxidase. The partitioning between catalytic oxidation of 2-hydroxy-3-butynoate and inactivation of the enzyme is determined by the concentration of the second substrate, 0 2 . Rapid reaction studies show the formation of an intermediate which is common to both the oxidation and inactivation pathways. This intermediate appears to be a charge-transfer complex between enzyme-reduced flavin and 2-keto-3-butynoate. It is characterized by a long-wavelength absorbing band ( A, , , 600 nm) and lack of fluorescence, making it easily distinguished from The use of acetylenic substrate analogues as specific irreversible inactivators of target enzymes was initiated by Bloch and his colleagues (Bloch, 1969), using 3-decynoyl thiolesters to inactivate /3-hydroxydecanoyl thiolester dehydrase. Specificity devolved from the fact that the enzyme converts the acetylenic molecule into a conjugated allenic thiolester, the actual alkylating agent, a t its active site. Subsequently, acetylenic analogues have been used to inactivate thiolase (Holland et al., 1973), plasma amine oxidase (Hevey et al., 1973), ketosteroid isomerase (Batzold and Robinson, 1 9 7 9 , and several pyridoxal phosphate-dependent enzymes (Abeles and Walsh, 1973;Marcotte and Walsh, 1975). In each instance carbanionic intermediates are suspected during catalysis, and covalent modification of some amino acid residue on the protein (apoprotein) is indicated.In addition several flavoenzymes can be induced to undergo irreversible inactivation by acetylenic analogues. Pargyline (N-benzyl-N-methylpropynylamine), long known to inhibit the flavin-linked monoamine oxidase (Hellerman and Erwin, 1968), appears to modify the FAD cofactor (Chuang et al., 1974). With N-dimethylpropynylamine as substrate, a covalent adduct forms a t N S of the flavin coenzyme (Maycock et al., 1976). In 1972 we reported the preliminary observation that the Mycobacterium smegmatis L-lactate oxidase is irreversibly inactivated by 2-hydroxy-3-butynoate due to covalent

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“…In addition it was our aim to determine the stereospecificity of the Pisum sativum enzyme by using chirally labeled glycollates and to compare it to the stereospecificity of other plant glycollate oxidases, which have been reported to be Respecific, or at least Re-selective [10,11]. GlycolIate oxidases from P. sativum [12] and human liver [13] have been reported to be inhibited by the suicide substrate a-hydroxybutynoic acid. With the human liver enzyme a-hydroxybutynoate was found to be a substrate and an irreversible inhibitor [13].…”

Section: Introduction Lytic Oxidation According To the Equationmentioning

confidence: 99%

Studies on glycollate oxidase from pea leaves determination of stereospecificity and mode of inhibition by α-hydroxybutynoate

Fendrich¹,

Ghisla²

1982

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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Inhibition of glycollate oxidase from pea leaves

Cited by 49 publications

References 12 publications

Photorespiratory Properties of Mesophyll Protoplasts of Nicotiana plumbaginifolia

Photorespiratory Properties of Mesophyll Protoplasts of Nicotiana plumbaginifolia

Kinetic studies on the inactivation of L-lactate oxidase by [the acetylenic suicide substrate]2-hydroxy-3-butynoate

Studies on glycollate oxidase from pea leaves determination of stereospecificity and mode of inhibition by α-hydroxybutynoate

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