Tomato alcohol dehydrogenase: Purification and substrate specificity

Bicsak, Thomas A.; Kann, Lance R.; Reiter, Andrew G.; Chase, Theodore

doi:10.1016/0003-9861(82)90250-8

Cited by 70 publications

(46 citation statements)

References 36 publications

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“…(c) class P is more constant than class I at the residues of the substrate binding regions, consistent with similar substrate specificity within plant species (Bicsak et al, 1982) and with a constant and specific function of class P in the plant kingdom, i.e. the reduction of acetaldehyde in the last step of alcoholic fermentation, contributing to the plant resistence to hypoxia.…”

Section: Molecular Patterns Alignments Of Plant Class I11 Structuressupporting

confidence: 69%

“…In the inner part of the substrate binding cleft, plant class P has Thr at position 48, as class I11 has, but human class I has a Ser. This Ser/Thr exchange may explain the low activity of plant ADHs toward secondary alcohols and cyclohexanol (Lai et al, 1982;Bicsak et al, 1982). In this inner part of the substrate binding cleft, all other residues of class P are identical or very similar to those of class I, explaining the ethanol activity and pyrazole inhibition common to these two alcohol dehydrogenase lines.…”

Section: I G N V S V M R a A L E C C H K G W G T S V I V G V A A Smentioning

confidence: 99%

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Arabidopsis Formaldehyde Dehydrogenase

Martínez

Achkor

Persson

et al. 1996

European Journal of Biochemistry

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A glutathione-dependent formaldehyde dehydrogenase (class I11 alcohol dehydrogenase) has been characterized from Arubidopsis thulium. This plant enzyme exhibits kinetic and molecular properties in common with the class I11 forms from mammals, with a K,, for S-hydroxymethylglutathione of 1.4 pM, an anodic electrophoretic mobility (PI: 5.3-5.6) and a cross-reaction with anti-(rat class I11 alcohol dehydrogenase) antibodies. The enzyme structure, deduced from the cDNA sequence, fits into the complex system of alcohol dehydrogenases and shows that all life forms share the class I11 protein type. The corresponding mRNA is 1.4 kb and present in all plant organs; a single copy of the gene is found in the genome. The class I11 structural variability is different from that of the ethanol-active enzyme types in both vertebrates (class I) and plants (class P), although class P conserves more of the class 111 properties than class I does. Also the enzymatic properties differ between the two ethanol-active classes. Activesite variability and exchanges at essential residues (Leu/Gly57, AsplArgll5) may explain the distinct kinetics. These patterns are consistent with two different metabolic roles for the ethanol-active enzymes, a more constant function, reduction of acetaldehyde during hypoxia, for class P, and a more variable function, the detoxication of alcohols and participation in metabolic conversions, for class I. A sequence motif, Pro-Xaa-IleNal-Xaa-Gly-His-Glu-Xaa-Xaa-Gly, common to all medium-chain alcohol dehydrogenases is defined.

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Section: Molecular Patterns Alignments Of Plant Class I11 Structuressupporting

confidence: 69%

Section: I G N V S V M R a A L E C C H K G W G T S V I V G V A A Smentioning

confidence: 99%

Arabidopsis Formaldehyde Dehydrogenase

Martínez

Achkor

Persson

et al. 1996

European Journal of Biochemistry

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“…3) the apparent K m for ethanol was determined to be 0.38 mM whereas the apparent K i for methanol was 5.1 mM. Methanol inhibition seems to be competitive much like pyrazole, a known inhibitor of ADH (10). Methanol was found to have no effect on tomato ADH activity in the absence of ethanol (data no shown) and has been found not to be a substrate for ADH in vitro in tomato or other plants (10).…”

Section: Methanol and Ethanol Accumulation In Ripening Tomatoes 4294mentioning

confidence: 96%

“…The 60% (NH 4 ) 2 SO 4 precipitate was resuspended in 50 mM Tris-HCl, pH 7.4, 5 mM dithiothreitol, and dialyzed against the same buffer overnight using dialysis tubing with a molecular weight cutoff of 6,000 to 8,000. The dialyzed solution was loaded onto a 1 ϫ 14 cm column of Cibacron blue (10), and the eluent was concentrated using an Amicon Centriprep 10 Ultrafiltration unit. ADH was purified 700-fold based on specific activity and consisted predominantly of ADH-2 isozyme and only traces of ADH-1 isozyme (10).…”

Section: Methodsmentioning

confidence: 99%

Pectin Methylesterase Regulates Methanol and Ethanol Accumulation in Ripening Tomato (Lycopersicon esculentum) Fruit

Frenkél¹,

Peters²,

Tieman³

et al. 1998

Journal of Biological Chemistry

109

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We provide genetic evidence that the production of methanol in tomato fruit is regulated by pectin methylesterase (PME, EC 3.1.1.11), an enzyme that catalyzes demethoxylation of pectins. The role of PME in methanol production in tomato fruit was examined by relating the tissue methanol content to the PME enzymatic activity in wild-type Rutgers and isogenic PME antisense fruits with lowered PME activity. In the wild-type, fruit development and ripening were accompanied by an increase in the abundance of PME protein and activity and a corresponding ripening-related increase in methanol content. In the PME antisense pericarp, the level of methanol was greatly reduced in unripe fruit, and diminished methanol content persisted throughout the ripening process. The close correlation between PME activity and levels of methanol in fruit tissues from wildtype and a PME antisense mutant indicates that PME is the primary biosynthetic pathway for methanol production in tomato fruit. Interestingly, ethanol levels that were low and unchanged during ripening of wild-type tomatoes increased progressively with the ripening of PME antisense fruit. In vitro studies indicate that methanol is a competitive inhibitor of the tomato alcohol dehydrogenase (ADH, EC 1.1.1.1) activity suggesting that ADH-catalyzed production of ethanol may be arrested by methanol accumulation in the wild-type but not in the PME mutant where methanol levels remain low.Methanol is emitted by actively growing plant tissues (1) and ripening fruit (2). A major source of methanol may be pectin methyl esters (3) that are de-esterified to methanol and pectic substances by a PME 1 -catalyzed reaction (4). Although methanol production is correlated with PME activity in germinating seeds or other plant tissues (1), the role of PME in methanol accumulation in plants has not been firmly established (4,5).A developmentally regulated increase in PME gene expression occurs in developing tomato fruit (6) and may be used as a test system to relate PME activity to methanol metabolism. We have created transgenic tomato fruits with severely impaired expression of PME by introducing a fruit-specific PME antisense gene under the control of cauliflower mosaic virus 35S promoter (7). We compared methanol production in the wildtype and the PME antisense tomato fruits to examine whether the arrest of PME gene expression results in diminished production of methanol. Our results show that methanol accumulation in ripening tomato pericarp of either the wild-type or the PME antisense is related to PME activity, suggesting that the PME activity is the primary source of methanol production in tomato fruits. A surprising finding is that the tissue methanol and ethanol content in ripening tomato fruit were inversely related.

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“…ADH is an oxidoreductase that catalyzes the reversible reduction of aldehydes to alcohols (68,113,114), and its direction is infl uenced by the pH. However, at physiological pH, the reaction favours the production of alcohols (29).…”

Section: Lipoxygenase Pathwaymentioning

confidence: 99%

Biochemistry of apple aroma: A review

Espino-Díaz¹,

Sepúlveda²,

González‐Aguilar

et al. 2016

Food Technol. Biotechnol.

146

134

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SummaryFlavour is a key quality att ribute of apples defi ned by volatile aroma compounds. Biosynthesis of aroma compounds involves metabolic pathways in which the main precursors are fatt y and amino acids, and the main products are aldehydes, alcohols and esters. Some enzymes are crucial in the production of volatile compounds, such as lipoxygenase, alcohol dehydrogenase, and alcohol acyltransferase. Composition and concentration of volatiles in apples may be altered by pre-and postharvest factors that cause a decline in apple fl avour. Addition of biosynthetic precursors of volatile compounds may be a strategy to promote aroma production in apples. The present manuscript compiles information regarding the biosynthesis of volatile aroma compounds, including metabolic pathways, enzymes and substrates involved, factors that may aff ect their production and also includes a wide number of studies focused on the addition of biosynthetic precursors in their production.

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Tomato alcohol dehydrogenase: Purification and substrate specificity

Cited by 70 publications

References 36 publications

Arabidopsis Formaldehyde Dehydrogenase

Arabidopsis Formaldehyde Dehydrogenase

Pectin Methylesterase Regulates Methanol and Ethanol Accumulation in Ripening Tomato (Lycopersicon esculentum) Fruit

Biochemistry of apple aroma: A review

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