Evaluation of the impact of functional diversification on Poaceae, Brassicaceae, Fabaceae, and Pinaceae alcohol dehydrogenase enzymes

Abstract

The plant alcohol dehydrogenases (ADHs) have been intensively studied in the last years in terms of phylogeny and they have been widely used as a molecular marker. However, almost no information about their three-dimensional structure is available. Several studies point to functional diversification of the ADH, with evidence of its importance, in different organisms, in the ethanol, norepinephrine, dopamine, serotonin, and bile acid metabolism. Computational results demonstrated that in plants these enzymes are submitted to a functional diversification process, which is reinforced by experimental studies indicating distinct enzymatic functions as well as recruitment of specific genes in different tissues. The main objective of this article is to establish a correlation between the functional diversification occurring in the plant alcohol dehydrogenase family and the three-dimensional structures predicted for 17 ADH belonging to Poaceae, Brassicaceae, Fabaceae, and Pinaceae botanical families. Volume, molecular weight and surface areas are not markedly different among them. Important electrostatic and pI differences were observed with the residues responsible for some of them identified, corroborating the function diversification hypothesis. These data furnish important background information for future specific structure-function and evolutionary investigations.

Leaf:fruit Ratio Affects the Proteomic Profile of Grape Berry Skins

“…Understanding the effect of increased LF ratio on these proteins, especially malate dehydrogenase, may be the key to understanding the link between increased acidity and high cropload as was seen in this study. In the group of fermentation proteins identified (function 02.16), two isoforms of alcohol dehydrogenase (spots 39, 46), which catalyze a reaction as part of fermentation to ensure a constant supply of NAD + (Thompson et al, 2010), were down-regulated by high cropload. Although grouped in the photosynthesis category (function 02.30), transketolase (spots 9, 10) is an enzyme of both the Calvin cycle of photosynthesis and the pentose phosphate pathway.…”

The plant ADH gene family

“…The same group also compared predicted 3D structures for a number of ADH enzymes and calculated theoretical isoelectric points. The pI values were higher for ADH1‐type isoforms than for their ADH2 counterparts in all cases (mean pI 6.30 versus 5.76; Thompson et al. , 2010).…”

A novel zinc‐binding alcohol dehydrogenase 2 from Arachis diogoi, expressed in resistance responses against late leaf spot pathogen, induces cell death when transexpressed in tobacco

“…During anaerobic glycolysis i.e., fermentation, ADH diverts the formation of lactic acid from pyruvate to less toxic and more diffusible ethanol, thereby helping cells to survive in the absence of oxygen required for normal respiration. Available evidences suggest that plant ADH gene family comprises survivors of multiple rounds of gene expansion and contraction resulting in gains in roles like production of characteristic scents that act to attract animals, pollinators, or agents of seed dispersal and to protect plants against herbivores besides anaerobic fermentation [1,2].…”

“…They are found in all plants, playing important roles in plant growth, pollen, and seedling development and fruit ripening 1, 2. They are well‐studied members of the medium‐length dehydrogenase/reductase (MDR) protein superfamily 3.…”

“…Zinc-binding alcohol dehydrogenases are NAD(P)dependent oxidoreductases involved in hydride ion transfer from alcohols to NAD + catalyzing reversible oxidation of alcohols to aldehydes or ketones. They are found in all plants, playing important roles in plant growth, pollen, and seedling development and fruit ripening [1,2]. They are well-studied members of the medium-length dehydrogenase/reductase (MDR) protein superfamily [3].…”