A myoglobin evolved from indoleamine 2,3-dioxygenase, a tryptophan-degrading enzyme

• Published in: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology Vol. 121; no. 2; pp. 117 - 128
• Main Authors: Suzuki, Tomohiko, Kawamichi, Hozumi, Imai, Kiyohiro
• Format: Book Review Journal Article
• Language: English
• Published: England Elsevier Inc 01.10.1998
• Subjects: Amino Acid Sequence; Animals; Autoxidation; Base Sequence; DNA, Complementary - genetics; Evolution; Evolution, Molecular; Gene structure; Hemoglobin; Humans; Indoleamine 2,3-dioxygenase; Indoleamine-Pyrrole 2,3,-Dioxygenase; Molecular Sequence Data; Mollusca - genetics; Mollusca - metabolism; Myoglobin; Myoglobin - chemistry; Myoglobin - genetics; Myoglobin - metabolism; Oxygen-binding property; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Spectral property; Tryptophan - metabolism; Tryptophan Oxygenase - chemistry; Tryptophan Oxygenase - genetics; Tryptophan Oxygenase - metabolism; Myoglobin; Autoxidation; Spectral property; Gene structure; Hemoglobin; Oxygen-binding property; Amino acid sequence; Indoleamine 2,3-dioxygenase; Evolution
• ISSN: 1096-4959; 1879-1107
• DOI: 10.1016/S0305-0491(98)10086-X

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.