Adenosylcobalamin-dependent methylmalonyl-CoA mutase isozymes in the photosynthetic protozoon Euglena gracilis Z

Watanabe, Fumio; Abe, K.; Tamura, Yoshiyuki; Nakano, Yoshihisa

doi:10.1099/00221287-142-9-2631

Cited by 11 publications

(7 citation statements)

References 2 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Moreover, the newly uncovered methionine-related B 12 dependence that is shared between some algae and animals (21) would constitute an additional B 12 -dependent step in the eukaryote common ancestor (at least under some growth conditions) because the plant and animal lineages also lie on opposite sides of the presently accepted eukaryotic root (39). Similar reasoning applies to B 12 -dependent methylmalonyl-CoA mutase in animals and Euglena (22). From this it would not, however, follow that the eukaryote ancestor was capable of B 12 synthesis, because many B 12 -dependent microbes are B 12 auxotrophs (15), which obtain the vitamin from the environment.…”

Section: Discussionmentioning

confidence: 92%

“…However, supplementing B12-deficient growth media with methionine could not restore normal Lobomonas growth levels (21), indicating the presence of additional B12-dependent steps. B12 dependence in Euglena relates to its B12-dependent ribonucleotide reductase (13,14) and methylmalonyl-CoA mutase (22), which likely form the basis of the classical Euglena clinical assay for diagnosing human B12 deficiency and for quantifying human serum B12 levels (23).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Euglena gracilis Ribonucleotide Reductase

Torrents

Trevisiol

Rotte

et al. 2006

Journal of Biological Chemistry

View full text Add to dashboard Cite

Ribonucleotide reductases provide the building blocks for DNA synthesis. Three classes of enzymes are known, differing widely in amino acid sequence but with similar structural motives and allosteric regulation. Class I occurs in eukaryotes and aerobic prokaryotes, class II occurs in aerobic and anaerobic prokaryotes, and class III occurs in anaerobic prokaryotes. The eukaryote Euglena gracilis contains a class II enzyme (Gleason, F. K., and Hogenkamp, H. P. (1970) J. Biol. Chem. 245, 4894 -4899) and, thus, forms an exception. Class II enzymes depend on vitamin B 12 for their activity. We purified the reductase from Euglena cells, determined partial peptide sequences, identified its cDNA, and purified the recombinant enzyme. Its amino acid sequence and general properties, including its allosteric behavior, were similar to the class II reductase from Lactobacillus leichmannii. Both enzymes belong to a distinct small group of reductases that unlike all other homodimeric reductases are monomeric. They compensate the loss of the second polypeptide of dimeric enzymes by a large insertion in the monomeric chain. Data base searching and sequence comparison revealed a homolog from the eukaryote Dictyostelium discoideum as the closest relative to the Euglena reductase, suggesting that the class II enzyme was present in a common, B 12 -dependent, eukaryote ancestor.

show abstract

Section: Discussionmentioning

confidence: 92%

mentioning

confidence: 99%

Euglena gracilis Ribonucleotide Reductase

Torrents

Trevisiol

Rotte

et al. 2006

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Crude cell extracts of E. gracilis have been reported to contain methylmalonyl-CoA mutase activity (67), leading the authors to suggest that this organism contains a third vitamin B 12 -dependent enzyme. This enzyme catalyzes the reversible conversion of succinyl-CoA to methylmalonyl-CoA.…”

Section: Cobalaminmentioning

confidence: 99%

Algae Need Their Vitamins

2006

View full text Add to dashboard Cite

“…Thus, MCM is the key enzyme for the photoassimilation of propionate in this organism. Euglena MCM activity is significantly higher in propionate-adapted cells than in photoautotrophic cells (Watanabe et al 1996). The Euglena MCM apoenzyme accumulated significantly at the end of the logarithmic growth phase (Miyamoto et al 2010).…”

Section: Vitamin B12mentioning

confidence: 93%

Biochemistry and Physiology of Vitamins in Euglena

Watanabe

Yoshimura

Shigeoka

2017

Advances in Experimental Medicine and Biology

View full text Add to dashboard Cite

Euglena gracilis Z requires vitamins B1 and B12 for growth. It takes up and accumulates large amounts of these exogenous vitamins through energy-dependent active transport systems. Except for these essential vitamins, E. gracilis Z has the ability to synthesize all human vitamins. Euglena synthesizes high levels of antioxidant vitamins such as vitamins C and E, and, thus, are used as nutritional supplements for humans and domestic animals. Methods to effectively produce vitamins in Euglena have been investigated.Previous biochemical studies indicated that E. gracilis Z contains several vitamin-related novel synthetic enzymes and metabolic pathways which suggests that it is a highly suitable organism for elucidating the physiological functions of vitamins in comparative biochemistry and biological evolution. E. gracilis Z has an unusual biosynthetic pathway for vitamin C, a hybrid of the pathways found in animals and plants. This chapter presents up-to-date information on the biochemistry and physiological functions of vitamins in this organism.

show abstract

Adenosylcobalamin-dependent methylmalonyl-CoA mutase isozymes in the photosynthetic protozoon Euglena gracilis Z

Cited by 11 publications

References 2 publications

Euglena gracilis Ribonucleotide Reductase

Euglena gracilis Ribonucleotide Reductase

Algae Need Their Vitamins

Biochemistry and Physiology of Vitamins in Euglena

Contact Info

Product

Resources

About