Molecular characterization of a bifunctional glyoxylate cycle enzyme, malate synthase/isocitrate lyase, in Euglena gracilis

Nakazawa, Masami; Minami, Tomomi; Teramura, Koji; Kumamoto, Shohei; Hanato, Sayaka; Takenaka, Shigeo; Ueda, Mitsuhiro; Inui, Hiroshi; Nakano, Yoshihisa; Miyatake, Kazutaka

doi:10.1016/j.cbpc.2005.05.006

Cited by 23 publications

(34 citation statements)

References 31 publications

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“…The bifunctional protein, called glyoxylate cycle enzyme (also known as the bifunctional glyoxylate cycle enzyme, malate synthase/isocitrate lyase) (Liu et al 1995(Liu et al , 1997, is a fusion protein with ICL and MS domains. The N-terminal domain (amino acids 1-519) of Euglena glyoxylate cycle enzyme has high sequence similarity to other MS enzymes and the C-terminal domain (amino acids 597-1165) is related to ICL family proteins (Nakazawa et al 2005). Despite the resemblance of the C-terminal domain to ICLs it was not possible to yield ICL activity by expression of the domain in E. coli.…”

Section: Glyoxylate Cyclementioning

confidence: 98%

The Mitochondrion of Euglena gracilis

Zimorski

Rauch

Hellemond

et al. 2017

Advances in Experimental Medicine and Biology

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In the presence of oxygen, Euglena gracilis mitochondria function much like mammalian mitochondria. Under anaerobiosis, E. gracilis mitochondria perform a malonyl-CoA independent synthesis of fatty acids leading to accumulation of wax esters, which serve as the sink for electrons stemming from glycolytic ATP synthesis and pyruvate oxidation. Some components (enzymes and cofactors) of Euglena's anaerobic energy metabolism are found among the anaerobic mitochondria of invertebrates, others are found among hydrogenosomes, the H-producing anaerobic mitochondria of protists.

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Section: Glyoxylate Cyclementioning

confidence: 98%

The Mitochondrion of Euglena gracilis

Zimorski

Rauch

Hellemond

et al. 2017

Advances in Experimental Medicine and Biology

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“…Mitochondrial localization of glyoxylate pathway enzymes is rare; two examples are the larvae of the nematodes Turbatrix aceti (McKinley and Trelease 1978) and Ascaris suum (Rubin and Trelease 1976). Nakazawa et al (2005) demonstrated that purified MS from E. gracilis also catalyzed the ICL reaction. Molecular cloning of the enzyme (Nakazawa et al 2005) revealed that E. gracilis has a bifunctional glyoxylate cycle enzyme having both ICL and MS domains on a single polypeptide.…”

Section: Novel Features Of the Glyoxylate Pathway In E Gracilismentioning

confidence: 98%

C2 metabolism in Euglena

Nakazawa

2017

Advances in Experimental Medicine and Biology

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Euglenoids are able to assimilate fatty acids and alcohols with various carbon-chain lengths, and ethanol is known to be one of the best carbon sources to support the growth of Euglena gracilis. Ethanol is first oxidized to acetate by the sequential reactions of alcohol dehydrogenase and acetaldehyde dehydrogenase in the mitochondria, and then converted to acetyl coenzyme A (acetyl-CoA). Acetyl-CoA is metabolized through the glyoxylate cycle which is a modified tricarboxylic acid (TCA) cycle in which isocitrate lyase (ICL) and malate synthase (MS) function to bypass the two decarboxylation steps of the TCA cycle, enabling the net synthesis of carbohydrates from C2 compounds. ICL and MS form a unique bifunctional enzyme localized in Euglena mitochondria, not in glyoxysome as in other eukaryotes. The unique glyoxylate and glycolate metabolism during photorespiration is also discussed in this chapter.

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“…Malate synthase activity was measured according to Cook [1,24].MS reaction, the synthesis reaction of acetylCoA and glyoxylate to L-malate, was assayed by measuring the degradation of acetyl-CoA at 30 o C.The reaction mixture of 1 mL volume consisted 100 mM Tris-HCl buffer, pH 8.0,10 mM MgCl2, 1 mM glyoxylate,150 μM acetyl-CoA, and the enzyme solution. The reaction was started by the addition of acetyl-CoA.…”

Section: B Enzyme Assays and Determination Of Protein Concentrationmentioning

confidence: 99%

“…The gloxylate cycle, which was first proposed by Kornberg and Krebs [1,2] in bacteria growing on acetate [3], is an anaplerotic metabolic pathway which plays an important role in the biogenesis of carbohydrates from C2 compounds [4,5].There are alternative pathways to the glyoxylate cycle in some bacteria [6][7][8].This pathway is widespread in living organisms (Bacteria, Eukarya and Archaea), and the two key enzymes (isocitrate lyase and malate synthase) have been detected in various eubacteria, fungi, plants and even some animals [4,6].…”

Section: Introductionmentioning

confidence: 99%

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Relationship between Glyoxylate Cycle and Nitrification Efficiency based on Heterotrophic Nitrification Bacterium Acinetobacter sp.Y1

Li¹,

Liu²

2017

Proceedings of the 2nd 2016 International Conference on Sustainable Development (ICSD 2016)

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Abstract-The growth and ammonium removal ability of heterotrophic nitrification bacterium are strongly influenced by carbon sources, as well as the activities of key enzymes of glyoxylate cycle. To obtain a better insight into the relationship between glyoxylate cycle and nitrification, the two key enzymes of glyoxylate cycle and the ammonium removal ability of Acinetobacter sp.Y1 grew with different carbon sources were examined. Strain Y1 showed a wide organic carbon substrates, and grew but no nitrify in the medium with sucrose and glycerol as sole carbon source. The strain Y1 showed the most activities of isocitrate lyase and malate synthase when the ammonium removal rate reached highest, and no activities of the two enzymes were detected when the strain grew without nitrification phase. The positive correlation relationship was found between the glyoxylate cycle and nitrification.

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Molecular characterization of a bifunctional glyoxylate cycle enzyme, malate synthase/isocitrate lyase, in Euglena gracilis

Cited by 23 publications

References 31 publications

The Mitochondrion of Euglena gracilis

The Mitochondrion of Euglena gracilis

C2 metabolism in Euglena

Relationship between Glyoxylate Cycle and Nitrification Efficiency based on Heterotrophic Nitrification Bacterium Acinetobacter sp.Y1

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