Purification and Properties of Betaine Aldehyde Dehydrogenase Extracted from Detached Leaves of Amaranthus hypochondriacus L. Subjected to Water Deficit

Valenzuela‐Soto, Elisa M.; Muñoz‐Clares, Rosario A.

doi:10.1016/s0176-1617(11)81678-0

Cited by 54 publications

(44 citation statements)

References 26 publications

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“…HvAMADH2, which also contains a cysteine, exhibits a good BAL activity (18). Moreover, AMADHs from members of the Amaranthaceae family (amaranth, spinach, and sugarbeet), from several monocots like barley or wheat, and from several grasses like sorghum or velvetgrass, known for their high BADH activity, possess such a cysteine (or an alanine) (49,50,10,51). The low or negligible BADH activity of ZmAMADH1b, ZmAMADH2, SlAMADH2, and PsAMADHs correlates with the presence of Ile-444 (Table 5).…”

Section: Role Of Trp-288 and Tyr-163 In Catalysis Of Aliphatic And Armentioning

confidence: 99%

Plant ALDH10 Family

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Tylichová

et al. 2013

Journal of Biological Chemistry

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Background: Plant aminoaldehyde dehydrogenases (AMADHs) detoxify -aminoaldehydes from several metabolic pathways. Results: Two of five new AMADHs exhibit unusual kinetic properties. A thiohemiacetal intermediate was trapped in a crystal structure. Conclusion: Five critical residues can modulate substrate specificity, and a new substrate was identified. Significance: The present findings allow sequence-based predictions of AMADH substrate specificity linked with the production of individual osmoprotectants in plants.

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Section: Role Of Trp-288 and Tyr-163 In Catalysis Of Aliphatic And Armentioning

confidence: 99%

Plant ALDH10 Family

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Tylichová

et al. 2013

Journal of Biological Chemistry

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“…A. tricolor is a major variety for vegetable and ornamental crops, and is widely cultivated in the world. Osmoprotectant glycine betaine (GB) was detected in Amaranthaceae, A. Hypochondriacus L [2] and A. Caudatus L [3], [4]. GB is widespread and an effective osmoprotectant in many plants [3].…”

Section: Introductionmentioning

confidence: 99%

“…CMO was assumed to be unique among plant oxygenases [6], [8]. The second step of GB synthesis is mediated by betaine aldehyde dehydrogenase (BADH) [1], which has been well documented in amaranth [2], [9] and other plants [10][11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Isolation of a choline monooxygenase cDNA clone from Amaranthus tricolor and its expressions under stress conditions

Meng

Zhang

et al. 2001

Cell Res

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Plants synthesize the osmoprotectant glycine betaine (GB) via choline betaine aldehyde glycine betaine [1]. Two enzymes are involved in the pathway, choline monooxygenase (CMO) and betaine aldehyde dehydrogenase (BADH). A full length CMO cDNA (1,643bp) was cloned from Amaranthus tricolor. The open reading frame encoded a 442-amino acid polypeptide, which showed 69% identity with CMOs in Spinacia oleracea L. and Beta vulgaris L. DNA gel blot analysis indicated the presence of one copy of CMO gene in the A. tricolor genome. The expressions of CMO and BADH proteins in A.tricolor leaves significantly increased under salinization, drought and heat stress (42 o C), as determined by immunoblot analysis, but did not respond to cold stress (4 o C), or exogenous ABA application. The increase of GB content in leaves was parallel to CMO and BADH contents.

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“…Some plants synthesize and accumulate glycine betaine (GB), the most efficient osmoprotector known (Courtenay et al, 2000), when subjected to osmotic stress (Hanson and Wyse, 1982;Yancey et al, 1982;Valenzuela-Soto and Muñ oz-Clares, 1994). It is generally accepted that GB is synthesized in the chloroplast stroma, as it is in spinach (Spinacia oleracea; Hanson et al, 1985), by a two-step oxidation of choline: first the alcohol group of choline is oxidized to the aldehyde group of betaine aldehyde (BAL) in a reaction catalyzed by choline monooxygenase (EC1.14.15.7; CMO), an enzyme unique to plants (Burnet et al, 1995); then the aldehyde group of BAL is oxidized to the acid group of GB in a reaction catalyzed by plant betaine aldehyde dehydrogenase [betaine aldehyde:NAD(P) + oxidoreductase (EC 1.2.1.8); BADH; Hanson et al, 1985;Arakawa et al, 1987;Valenzuela-Soto and Muñ oz-Clares, 1994;Burnet et al, 1995;Hibino et al, 2001;Nakamura et al, 2001;Fujiwara et al, 2008;Kopěcný et al, 2011], an enzyme that belongs to the aldehyde dehydrogenase family10 (ALDH10; Vasiliou et al, 1999). Engineering the synthesis of GB in crops that naturally lack this ability has been a biotechnological goal for improving tolerance to osmotic stress (McNeil et al, 1999;Rontein et al, 2002;Waditee et al, 2007).…”

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Amino Acid Residues Critical for the Specificity for Betaine Aldehyde of the Plant ALDH10 Isoenzyme Involved in the Synthesis of Glycine Betaine

et al. 2012

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Plant Aldehyde Dehydrogenase10 (ALDH10) enzymes catalyze the oxidation of v-primary or v-quaternary aminoaldehydes, but, intriguingly, only some of them, such as the spinach (Spinacia oleracea) betaine aldehyde dehydrogenase (SoBADH), efficiently oxidize betaine aldehyde (BAL) forming the osmoprotectant glycine betaine (GB), which confers tolerance to osmotic stress. The crystal structure of SoBADH reported here shows tyrosine (Tyr)-160, tryptophan (Trp)-167, Trp-285, and Trp-456 in an arrangement suitable for cation-p interactions with the trimethylammonium group of BAL. Mutation of these residues to alanine (Ala) resulted in significant K m (BAL) increases and V max /K m (BAL) decreases, particularly in the Y160A mutant. Tyr-160 and Trp-456, strictly conserved in plant ALDH10s, form a pocket where the bulky trimethylammonium group binds. This space is reduced in ALDH10s with low BADH activity, because an isoleucine (Ile) pushes the Trp against the Tyr. Those with high BADH activity instead have Ala (Ala-441 in SoBADH) or cysteine, which allow enough room for binding of BAL. Accordingly, the mutation A441I decreased the V max /K m (BAL) of SoBADH approximately 200 times, while the mutation A441C had no effect. The kinetics with other v-aminoaldehydes were not affected in the A441I or A441C mutant, demonstrating that the existence of an Ile in the second sphere of interaction of the aldehyde is critical for discriminating against BAL in some plant ALDH10s. A survey of the known sequences indicates that plants have two ALDH10 isoenzymes: those known to be GB accumulators have a high-BAL-affinity isoenzyme with Ala or cysteine in this critical position, while non GB accumulators have low-BAL-affinity isoenzymes containing Ile. Therefore, BADH activity appears to restrict GB synthesis in non-GB-accumulator plants.

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Purification and Properties of Betaine Aldehyde Dehydrogenase Extracted from Detached Leaves of Amaranthus hypochondriacus L. Subjected to Water Deficit

Cited by 54 publications

References 26 publications

Plant ALDH10 Family

Plant ALDH10 Family

Isolation of a choline monooxygenase cDNA clone from Amaranthus tricolor and its expressions under stress conditions

Amino Acid Residues Critical for the Specificity for Betaine Aldehyde of the Plant ALDH10 Isoenzyme Involved in the Synthesis of Glycine Betaine

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