Functional assignment of Glu386 and Arg388 in the active site of <scp>l</scp>‐galactono‐γ‐lactone dehydrogenase

Leferink, Nicole G. H.; Jose, Mac Donald F.; Berg, W.A.M. van den; Berkel, Willem J.H. van

doi:10.1016/j.febslet.2009.09.004

Cited by 22 publications

(21 citation statements)

References 21 publications

(36 reference statements)

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“…5,8,16 Our findings are in agreement with the suggestion of Massey et al that positively charged residue(s) in the vicinity of the flavin would not only stabilize the anionic semiquinone (SQ), or anionic hydroquinone (HQ), but also promote sulfite binding and sulfite attack on N (5) of the oxidized flavin, 22 which has also been nicely demonstrated by site-directed mutagenesis studies on L-galactono-γ-lactone dehydrogenase. 27 …”

Section: Structure Of T169s With Bound Acetatementioning

confidence: 97%

H-Bonding and Positive Charge at the N(5)/O(4) Locus Are Critical for Covalent Flavin Attachment in Trametes Pyranose 2-Oxidase

Tan

Pitsawong

Wongnate

et al. 2010

Journal of Molecular Biology

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Section: Structure Of T169s With Bound Acetatementioning

confidence: 97%

H-Bonding and Positive Charge at the N(5)/O(4) Locus Are Critical for Covalent Flavin Attachment in Trametes Pyranose 2-Oxidase

Tan

Pitsawong

Wongnate

et al. 2010

Journal of Molecular Biology

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“…The functional role of the Glu-Arg pair in the catalytic domain, conserved among aldonolactone oxidoreductases, was studied in AtGLDH by site-directed mutagenesis (Leferink et al, 2009c). It was demonstrated that this pair is essential for optimal catalysis.…”

Section: Active Site Inhibitors and Functional Residues Of Aldonmentioning

confidence: 99%

“…The Arg-388 residue is essential for the stabilization of negative charge resulting from flavin reduction. An Arg388Lys variant showed some activity while the Arg388Ala variant was essentially inactive (Leferink et al, 2009c). This pair is also widely conserved among all aldonolactone oxidoreductases with the exception of AtGulLO5 and P. griseoroseum GUO (Figure 2).…”

Section: Active Site Inhibitors and Functional Residues Of Aldonmentioning

confidence: 99%

“…Arrow indicates the cysteine residue known to be involved with thiol modifying agents in AtGLDH (Leferink et al 2009d). The Glu-Arg pair identified in the catalytic site of AtGLDH (Leferink et al 2009c) is also highlighted. The sequences used are: BoGLDH (cauliflower; Swiss-Prot: O47881), IbGLDH (sweet potato; GenBank: BAA34995), NtGLDH (tobacco; GenBank: BAB13368), AtGLDH ( Arabidopsis ; Swiss-Prot: Q9SU56), AtGulLO5 ( Arabidopsis ; GenBank: AEC10747), RnGulLO (rat; Swiss-Prot: P10867), MmGulLO (mouse; GenBank: AAR15891), SsGulLO (pig; GenBank: AAN63634), ScALO ( S. cerevisiae ; Swiss-Prot: P54783), CaALO ( C. albicans ; GenBank: AAC98913), PgGUO ( P. griseoroseum ; Swiss-Prot: Q671X8), TbGalLO ( T. brucei ; Swiss-Prot: Q57ZU1), TcGalLO ( T. cruzi ; Swiss-Prot: Q4DPZ5), LdALO ( L. donovani ; GenBank: ACV04074), MtGulLDH ( M. tuberculosis ; Swiss-Prot: O06804).…”

Section: Figurementioning

confidence: 99%

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Recent progress on the characterization of aldonolactone oxidoreductases

Aboobucker

Lorence

2016

Plant Physiology and Biochemistry

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l-Ascorbic acid (ascorbate, AsA, vitamin C) is essential for animal and plant health. Despite our dependence on fruits and vegetables to fulfill our requirement for this vitamin, the metabolic network leading to its formation in plants is just being fully elucidated. There is evidence supporting the operation of at least four biosynthetic pathways leading to AsA formation in plants. These routes use d-mannose/l-Galactose, l-gulose, d-galacturonate, and myo-inositol as the main precursors. This review focuses on aldonolactone oxidoreductases, a subgroup of the vanillyl alcohol oxidase (VAO; EC 1.1.3.38) superfamily, enzymes that catalyze the terminal step in AsA biosynthesis in bacteria, protozoa, animals, and plants. In this report, we review the properties of well characterized aldonolactone oxidoreductases to date. A shared feature in these proteins is the presence of a flavin cofactor as well as a thiol group. The flavin cofactor in many cases is bound to the N terminus of the enzymes or to a recently discovered HWXK motif in the C terminus. The binding between the flavin moiety and the protein can be either covalent or non-covalent. Substrate specificity and subcellular localization differ among the isozymes of each kingdom. All oxidases among these enzymes possess dehydrogenase activity, however, exclusive dehydrogenases are also found. We also discuss recent evidence indicating that plants have both l-gulono-1,4-lactone oxidases and l-Galactono-1,4-lactone dehydrogenases involved in AsA biosynthesis.

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“…327 2018) and L-GalLDH and AOX activities are sensitive to H 2 O 2(Leferink et al, 2009). Likely, H 2 O 2 also 328 plays a role in inactivating AOX pathway during AsA synthesis.…”

mentioning

confidence: 94%

Mitochondrial ascorbate synthesis acts as a pro-oxidant pathway and down-regulate energy supply in plants

Oliveira

Morales

Silva

et al. 2019

Preprint

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31Attempts to improve the ascorbate (AsA) content of plants are still dealing with the limited 32 understanding of why exists a wide variability of this powerful anti-oxidant molecule in different 33 plant sources, species and environmental situations. In plant mitochondria, the last step of AsA 34 synthesis is catalyzed by the enzyme L-galactone-1,4-lactone dehydrogenase (L-GalLDH). By using 35GalLDH-RNAi silencing plant lines, biochemical and proteomic approaches, we here discovered 36 that, in addition to accumulate this antioxidant, mitochondria synthesize AsA to down-regulate the 37 respiratory activity and the cellular energy provision. The work reveals that the AsA synthesis 38 pathway within mitochondria is a branched electron transfer process that channels electrons 39 towards the alternative oxidase, interfering with conventional electron transport. It was 40 unexpectedly found that significant hydrogen peroxide is generated during AsA synthesis, which 41 affects the AsA level. The induced AsA synthesis shows proteomic alterations of mitochondrial 42 and extra-mitochondrial proteins related to oxidative and energetic metabolism. The most 43 identified proteins were known components of plant responses to high light acclimation, 44 programmed cell death, oxidative stress, senescence, cell expansion, iron and phosphorus 45 starvation, different abiotic stress/pathogen attack responses and others. We propose that 46 changing the electron flux associated with AsA synthesis might be part of a new mechanism by 47 which the L-GalLDH enzyme would adapt plant mitochondria to fluctuating energy demands and 48 redox status occurring under different physiological contexts. 49 50 to mETC but via flavin dinucleotide (FAD) (Sweetlove et al., 2010). These oxidation reactions are all 60 coupled to reduction of the ubiquinone (UQ) to ubiquinol (UQH 2 ) (Schertl and Braun, 2014). 61

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Functional assignment of Glu386 and Arg388 in the active site of l‐galactono‐γ‐lactone dehydrogenase

Cited by 22 publications

References 21 publications

H-Bonding and Positive Charge at the N(5)/O(4) Locus Are Critical for Covalent Flavin Attachment in Trametes Pyranose 2-Oxidase

H-Bonding and Positive Charge at the N(5)/O(4) Locus Are Critical for Covalent Flavin Attachment in Trametes Pyranose 2-Oxidase

Recent progress on the characterization of aldonolactone oxidoreductases

Mitochondrial ascorbate synthesis acts as a pro-oxidant pathway and down-regulate energy supply in plants

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