A myoglobin evolved from indoleamine 2,3-dioxygenase, a tryptophan-degrading enzyme.
The distribution, isolation, spectral and oxygen-binding properties, stability of ferrous state (autoxidation), amino acid sequence and gene structure of indoleamine 2,3-dioxygenase (IDO)-like myoglobins are summarized, and their evolution is discussed. Although it has long been thought that all hemoglobins and myoglobins have evolved from a common ancestral gene encoding a 14-16 kDa polypeptide, the discovery of IDO-like myoglobin from several gastropod molluscs clearly indicates that there was an alternative pathway for myoglobin evolution.
Suzuki
T
T
Laboratory of Biochemistry, Faculty of Science, Kochi University, Japan. suzuki@cc.kochi-u.ac.jp
Kawamichi
H
H
Imai
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary / Q000235:genetics; D019143:Evolution, Molecular; D006801:Humans; D050503:Indoleamine-Pyrrole 2,3,-Dioxygenase; D008969:Molecular Sequence Data; D008974:Mollusca / Q000235:genetics / Q000378:metabolism; D009211:Myoglobin / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid; D014364:Tryptophan / Q000378:metabolism; D014366:Tryptophan Oxygenase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*