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Methyladeninylcobamide functions as the cofactor of methionine synthase in a Cyanobacterium, Spirulina platensis NIES‐39
Author(s) -
Tanioka Yuri,
Miyamoto Emi,
Yabuta Yukinori,
Ohnishi Kouhei,
Fujita Tomoyuki,
Yamaji Ryoichi,
Misono Haruo,
Shigeoka Shigeru,
Nakano Yoshihisa,
Inui Hiroshi,
Watanabe Fumio
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.06.013
Subject(s) - spirulina (dietary supplement) , cobalamin , cofactor , biochemistry , methionine , methionine synthase , chemistry , amino acid , methylcobalamin , homocysteine , enzyme , biology , vitamin b12 , raw material , organic chemistry
To clarify the physiological function of pseudovitamin B 12 (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.