Short-Chain Acyl-CoA-Dependent Production of Oxalate from Oxaloacetate by Burkholderia glumae, a Plant Pathogen Which Causes Grain Rot and Seedling Rot of Rice via the Oxalate Production

Li, Hui-Q.; Matsuda, Iwao; Fujise, Yutaka; Ichiyama, Arata

doi:10.1093/oxfordjournals.jbchem.a022429

Cited by 23 publications

(38 citation statements)

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“…1a). In contrast, our structural and functional analyses, together with a previous isotope labeling experiment (12), suggest that oxaloacetate is a nucleophile for ObcA. Fig.…”

Section: Discussioncontrasting

confidence: 66%

“…Previous biochemical studies propose that ObcA catalyzes the formation of a C6-CoA adduct between oxaloacetate (four-carbon compound) and acetyl-CoA (two-carbon acetyl moiety); in a subsequent and independent reaction, ObcB utilizes the C6-CoA adduct as a substrate to produce three different products (see Fig. 1a) (12). Substrate-labeling experiments further suggested …”

mentioning

confidence: 89%

“…1a) (12,13), even though these two enzymes utilize identical substrates. Unlike B. glumae, B. thailandensis catalyzes the two-step reaction with a single bifunctional enzyme, Obc1, which consists of an ObcA homolog (54% sequence identity) in its N-terminal domain (see Fig.…”

Section: )mentioning

confidence: 99%

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Structural basis for bacterial quorum sensing-mediated oxalogenesis

Goo

Hwang

et al. 2014

Acta Cryst Sect A

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Background: Oxalogenesis in the Burkholderia species is an indispensable event for their survival in the stationary phase. Results: Structural and functional analyses of ObcA, the first enzyme in oxalogenesis, unravel an unprecedented reaction mechanism. Conclusion: ObcA produces a tetrahedral CoA adduct. Significance: This study provides a structural basis for understanding the first step in oxalogenesis.

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“…1a). In contrast, our structural and functional analyses, together with a previous isotope labeling experiment (12), suggest that oxaloacetate is a nucleophile for ObcA. Fig.…”

Section: Discussioncontrasting

confidence: 66%

mentioning

confidence: 89%

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Structural basis for bacterial quorum sensing-mediated oxalogenesis

Goo

Hwang

et al. 2014

Acta Cryst Sect A

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“…From the literature surveyed, the metabolic system found in this investigation is the first example of metabolic coupling or interdependency of the [12]), see Table 1. TCA and GLOX cycles, which has never been reported from any other organism. However, Li et al (45) have discovered a different type of oxalate-producing system involving acetyl-CoA from the plant pathogen Burkholderia glumae. Moreover, ICL, which is shared by the two coupling cycles, is focused as a crucial enzyme for the oxalate biosynthesis in this fungus.…”

Section: Biochemical Role Of a Metabolic System For Biosynthesis Of Omentioning

confidence: 99%

A physiological role for oxalic acid biosynthesis in the wood-rotting basidiomycete Fomitopsis palustris

Munir

Yoon

Tokimatsu

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

149

112

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A metabolic mechanism for oxalic acid biosynthesis in the woodrotting basidiomycete Fomitopsis palustris has been proposed on the basis of biochemical analyses of glucose metabolism. There was a strong correlation between glucose consumption and oxalate production. Oxalic acid was found to accumulate in the culture fluid in about 80% of the theoretical yield or about 5-fold, on the basis of the fungal biomass harvested. The results clearly indicate that glucose was not completely oxidized to CO2 by the tricarboxylic acid (TCA) cycle but converted mainly to oxalate. The determination of the 12 enzymes concerned has revealed the occurrence of the unprecedented metabolic coupling of the TCA and glyoxylate cycles that support oxalate biosynthesis. In this metabolic system, isocitrate lyase (EC 4.1.3.1), together with oxaloacetase (EC 3.7.1.1), was found to play a pivotal role in yielding oxalate from oxaloacetate via the acetate-recycling routes. Moreover, malate dehydrogenase (EC 1.1.1.37), with an extraordinarily high activity among the enzymes tested, was shown to play an important role in generating NADH by oxidation of malate to oxaloacetate. Thus, it is proposed that the wood-rotting basidiomycete acquires biochemical energy by oxidizing glucose to oxalate.

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“…C, the N-domain is shown in a different orientation from that of panel B. The (␤/␣) 8 -barrel fold is within a circle. D, the topology of the ␣/␤ hydrolase fold in the Obc1 C-domain is shown.…”

Section: Resultsmentioning

confidence: 99%

Structural Insights into an Oxalate-producing Serine Hydrolase with an Unusual Oxyanion Hole and Additional Lyase Activity

Hwang

Rhee

2016

Journal of Biological Chemistry

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In Burkholderia species, the production of oxalate, an acidic molecule, is a key event for bacterial growth in the stationary phase. Oxalate plays a central role in maintaining environmental pH, which counteracts inevitable population-collapsing alkaline toxicity in amino acid-based culture medium. In the phytopathogen Burkholderia glumae, two enzymes are responsible for oxalate production. First, the enzyme oxalate biosynthetic component A (ObcA) catalyzes the formation of a tetrahedral C6-CoA adduct from the substrates acetyl-CoA and oxaloacetate. Then the ObcB enzyme liberates three products from the C6-CoA adduct: oxalate, acetoacetate, and CoA. Interestingly, these two stepwise reactions are catalyzed by a single bifunctional enzyme, Obc1, from Burkholderia thailandensis and Burkholderia pseudomallei. Obc1 has an ObcA-like N-terminal domain and shows ObcB activity in its C-terminal domain despite no sequence homology with ObcB. We report the crystal structure of Obc1 in its apo and glycerol-bound form at 2.5 Å and 2.8 Å resolution, respectively. The Obc1 N-terminal domain is essentially identical both in structure and function to that of ObcA. Its C-terminal domain has an ␣/␤ hydrolase fold that has a catalytic triad for oxalate production and a novel oxyanion hole distinct from the canonical HGGG motif in other ␣/␤ hydrolases. Functional analyses through mutagenesis studies suggested that His-934 is an additional catalytic acid/base for its lyase activity and liberates two additional products, acetoacetate and CoA. These results provide structural and functional insights into bacterial oxalogenesis and an example of divergent evolution of the ␣/␤ hydrolase fold, which has both hydrolase and lyase activity.

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Short-Chain Acyl-CoA-Dependent Production of Oxalate from Oxaloacetate by Burkholderia glumae, a Plant Pathogen Which Causes Grain Rot and Seedling Rot of Rice via the Oxalate Production

Cited by 23 publications

References 0 publications

Structural basis for bacterial quorum sensing-mediated oxalogenesis

Structural basis for bacterial quorum sensing-mediated oxalogenesis

A physiological role for oxalic acid biosynthesis in the wood-rotting basidiomycete Fomitopsis palustris

Structural Insights into an Oxalate-producing Serine Hydrolase with an Unusual Oxyanion Hole and Additional Lyase Activity

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