Isolation and Characterization of a New Vitamin C Producing Enzyme (<scp>L</scp>-Gulono-<i>γ</i>-lactone Dehydrogenase) of Bacterial Origin

Sugisawa, Teruhide; Ojima, Setsuko; Matzinger, Peter K.; Hoshino, Tatsuo

doi:10.1271/bbb.59.190

Cited by 28 publications

(28 citation statements)

References 4 publications

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“…Yeast isozymes can use D-AL in addition to L-GulL and L-GalL [13, 77]. Bacterial GulLDHs are specific to L-GulL and do not use L-GalL as substrate [14, 49]. Interestingly, our phylogenetic analysis shows AtGulLOs, including AtGulLO5 (specific to L-GulL) and GLDHs from plants (specific to L-GalL), in two separate clades (Figure 2B).…”

Section: Discussionmentioning

confidence: 99%

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Characterization of Two Arabidopsis L-Gulono-1,4-lactone Oxidases, AtGulLO3 and AtGulLO5, Involved in Ascorbate Biosynthesis

Aboobucker

Suza

Lorence

2017

ROS

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L-Ascorbic acid (AsA, vitamin C) is an essential antioxidant for plants and animals. There are four known ascorbate biosynthetic pathways in plants: the L-galactose, L-gulose, D-galacturonate, and myo-inositol routes. These pathways converge into two AsA precursors: L-galactono-1,4-lactone and L-gulono-1,4-lactone (L-GulL). This work focuses on the study of L-gulono-1,4-lactone oxidase (GulLO), the enzyme that works at the intersect of the gulose and inositol pathways. Previous studies have shown that feeding L-gulono-1,4-lactone to multiple plants leads to increased AsA. There are also reports showing GulLO activity in plants. We describe the first detailed characterization of a plant enzyme specific to oxidize L-GulL to AsA. We successfully purified a recombinant Arabidopsis GulLO enzyme (called AtGulLO5) in a transient expression system. The biochemical properties of this enzyme are similar to the ones of bacterial isozymes in terms of substrate specificity, subcellular localization, use of flavin adenine dinucleotide (FAD) as electron acceptor, and specific activity. AtGulLO5 is an exclusive dehydrogenase with an absolute specificity for L-GulL as substrate thus differing from the existing plant L-galactono-1,4-lactone dehydrogenases and mammalian GulLOs. Feeding L-GulL to N. benthamiana leaves expressing AtGulLO5 constructs led to increased foliar AsA content, but it was not different from that of controls, most likely due to the observed low catalytic efficiency of AtGulLO5. Similar results were also obtained with another member of the AtGulLO family (AtGulLO3) that appears to have a rapid protein turnover. We propose that AsA synthesis through L-GulL in plants is regulated at the post-transcriptional level by limiting GulLO enzyme availability.

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Section: Discussionmentioning

confidence: 99%

“…Similar to AtGulLO5, there are two exclusive dehydrogenases specific to L-GulL—among aldonolactone oxidoreductases—in G. oxydans [49], M. tuberculosis [14]. Plant GLDHs [17, 20] and E. gracilis GulLDH [76] are also exclusive dehydrogenases but their substrate specificities are different.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Two Arabidopsis L-Gulono-1,4-lactone Oxidases, AtGulLO3 and AtGulLO5, Involved in Ascorbate Biosynthesis

Aboobucker

Suza

Lorence

2017

ROS

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“…The GulLDH of Gluconobacter oxydans is reported to contain a cytochrome C component in addition to the flavin group (Sugisawa et al, 1995). The recombinant GulLDH of M. tuberculosis does not have a flavin cofactor, as no flavin spectrum was seen; in addition the enzyme was insensitive to exogenous FAD or riboflavin addition (Wolucka and Communi, 2006).…”

Section: Flavin Attachment To Aldonolactone Oxidoreductasesmentioning

confidence: 99%

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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“…An L-galactono-γ -lactone oxidase has also been isolated from baker's yeast, which catalyzes the conversion of both l-galactonolactone and L-gulonolactone to L-ascorbic acid (Nishikimi et al, 1980). The yield of vitamin C from yeast is low (Sugisawa et al, 1995), and it seems unlikely that this route will replace the more productive bacterial conversions in the near future.…”

Section: Other Routes To Vitamin Cmentioning

confidence: 99%

“…to be similar to those of 2-keto-D-gluconate dehydrogenase and D-sorbitol dehydrogenase of G. melasnogenus and G. suboxydans var α. L-Gulono-γ-lactone dehydrogenase was reported to give yields of ascorbic acid of 24.6 and 23.7% in growing and resting cells, respectively (Sugisawa et al, 1995). Like the yeast bioconversion route, so far, this process does not appear to be promising.…”

Section: Other Routes To Vitamin Cmentioning

confidence: 99%

The GenusGluconobacterand Its Applications in Biotechnology

Macauley

McNeil

Harvey

2001

Critical Reviews in Biotechnology

106

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Organisms of the genus Gluconobacter have been widely utilized within the biotechnology industry for many decades, due to their unique metabolic characteristics. The metabolic features that render Gluconobacter so useful in biotransformation processes, vitamin synthesis, and, as the biological element in sensor systems, are critically evaluated, and the relevance of recent biochemical genetic studies to current and future industrial Gluconobacter processes is discussed. The impact of recombinant gene technology on the status of Gluconobacter processes and the potential use of such techniques in clarifying aspects of the physiology of Gluconobacter is reviewed.

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Isolation and Characterization of a New Vitamin C Producing Enzyme (L-Gulono-γ-lactone Dehydrogenase) of Bacterial Origin

Cited by 28 publications

References 4 publications

Characterization of Two Arabidopsis L-Gulono-1,4-lactone Oxidases, AtGulLO3 and AtGulLO5, Involved in Ascorbate Biosynthesis

Characterization of Two Arabidopsis L-Gulono-1,4-lactone Oxidases, AtGulLO3 and AtGulLO5, Involved in Ascorbate Biosynthesis

Recent progress on the characterization of aldonolactone oxidoreductases

The GenusGluconobacterand Its Applications in Biotechnology

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