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Methyladeninylcobamide functions as the cofactor of methionine synthase in a Cyanobacterium, Spirulina platensis NIES-39 |
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| Authors: | Yuri Tanioka Emi Miyamoto Kouhei Ohnishi Ryoichi Yamaji Shigeru Shigeoka Hiroshi Inui |
| Affiliation: | a Department of Nutrition, Junior College of Tokyo University of Agriculture, Setagayaku, Tokyo156-8502, Japan b Department of Health and Nutrition, Nagasaki International University, Sasebo, Japan c School of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori, Japan d Research Institute of Molecular Genetics, Kochi University, Nankoku, Japan e Graduate School of Agriculture, Shinshu University, Nagano, Japan f Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Sakai, Japan g Department of Advanced Biosciences, Kochi University, Nankoku, Japan h Department of Advanced Bioscience, Kinki University, Nara, Japan |
| Abstract: | To clarify the physiological function of pseudovitamin B12 (or adeninylcobamide; AdeCba) in Spirulina platensis NIES-39, cobalamin-dependent methionine synthase (MS) was characterized. We cloned the full-length Spirulina MS. The clone contained an open reading frame encoding a protein of 1183 amino acids with a molecular mass of 132 kDa. Deduced amino acid sequences of the Spirulina MS contained critical residues identical to cobalamin-, zinc-, S-adenosylmethionine-, and homocysteine-binding motifs. The recombinant Spirulina enzyme showed higher affinity for methyladeninylcobamide than methylcobalamin as a cofactor. These results indicate that Spirulina cells can utilize AdeCba synthesized as the cofactor for MS. |
| Keywords: | AdeCba, adeninylcobamide AdoMet, S-adenosylmethionine Cbl, cobalamin CH3-AdeCba, methyladeninylcobamide CH3-Cbl, methylcobalamin CN-AdeCba, cyanoadeninylcobamide or pseudovitamin B12 MS, methionine synthase SDS, sodium dodecyl sulfate |
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