Methyladeninylcobamide functions as the cofactor of methionine synthase in a Cyanobacterium, Spirulina platensis NIES-39

FEBS Letters

Volumn 584, Issue 14, 2010, Pages 3223-3226

  Tanioka, Yuri ^a   Miyamoto, Emi ^b   Yabuta, Yukinori ^c   Ohnishi, Kouhei ^d   Fujita, Tomoyuki ^e   Yamaji, Ryoichi ^f   Misono, Haruo ^d   Shigeoka, Shigeru ^g   Nakano, Yoshihisa ^f   Inui, Hiroshi ^f   Watanabe, Fumio ^c  

^a TOKYO UNIVERSITY OF AGRICULTURE   (Japan)

^b NAGASAKI INTERNATIONAL UNIVERSITY   (Japan)

^c TOTTORI UNIVERSITY   (Japan)

^d KOCHI UNIVERSITY   (Japan)

^e SHINSHU UNIVERSITY   (Japan)

^f Osaka Prefecture University   (Japan)

^g KINKI UNIVERSITY   (Japan)

Author keywords

Adeninylcobamide; Cobalamin; Cyanobacteria; Methionine synthase; Pseudovitamin B12; Spirulina platensis

Indexed keywords

ADENINYLCOBAMIDE; COBALAMIN; COBALAMIN DERIVATIVE; HOMOCYSTEINE; MECOBALAMIN; METHIONINE SYNTHASE; METHYLADENINYLCOBAMIDE; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG; ZINC; 5 METHYLTETRAHYDROFOLATE HOMOCYSTEINE METHYLTRANSFERASE; CYANOCOBALAMIN; DRUG DERIVATIVE; INORGANIC COMPOUND; ORGANIC COMPOUND;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL METABOLISM; BACTERIAL STRAIN; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME ISOLATION; ENZYME SYNTHESIS; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN MOTIF; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SPIRULINA PLATENSIS; BACTERIUM; CHEMISTRY; CYANOBACTERIUM; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE;

CYANOBACTERIA; SPIRULINA; SPIRULINA PLATENSIS;

5-METHYLTETRAHYDROFOLATE-HOMOCYSTEINE S-METHYLTRANSFERASE; AMINO ACID SEQUENCE; BACTERIA; CYANOBACTERIA; INORGANIC CHEMICALS; MOLECULAR SEQUENCE DATA; ORGANIC CHEMICALS; PROTEIN STRUCTURE, TERTIARY; S-ADENOSYLMETHIONINE; VITAMIN B 12;

EID: 77954175019     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.06.013     Document Type: Article

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