PMID- 19402226
OWN - NLM
STAT- MEDLINE
DCOM- 20090615
LR  - 20131121
IS  - 1879-1107 (Electronic)
IS  - 1096-4959 (Linking)
VI  - 153
IP  - 2
DP  - 2009 Jun
TI  - Characterization and evolution of vertebrate indoleamine 2, 3-dioxygenases IDOs 
      from monotremes and marsupials.
PG  - 137-44
AB  - Indoleamine 2,3-dioxygenase (IDO1) and tryptophan 2,3-dioxygenase (TDO) are 
      tryptophan-degrading enzymes that catalyze the first step in tryptophan 
      catabolism via the kynurenine pathway. TDO is widely distributed in both 
      eukaryotes and bacteria. In contrast, IDO has been found only in mammals and 
      yeast. In 2007, a third enzyme, indoleamine 2,3-dioxygenase-2 (IDO2), was 
      discovered. IDO2 is found not only in mammals but also in lower vertebrates. 
      Interestingly, the Km value of IDO2 for L-Trp was 500-1000 fold higher than that 
      of IDO1. In this study, we isolated both IDO1 and IDO2 cDNA from a monotreme, the 
      platypus (Ornithorhynchus anatinus), and a marsupial, the gray short-tailed 
      opossum (Monodelphis domestica). We characterized the recombinant proteins and 
      those of other known IDO1/IDO2 in intact cells and a cell-free system. It was 
      found that methylene blue may not be suitable reductant for IDO2, hence resulting 
      in an underestimation of recombinant IDO2 activity. In intact cells, the Km value 
      of IDO2 for L-Trp was estimated to be much higher than that of IDO1 and this high 
      Km value appears to have been conserved during the evolution of IDO2. The protein 
      encoded by the ancestor gene of IDO1 and IDO2 is likely to have had properties 
      more similar to present day IDO2 than to IDO1.
FAU - Yuasa, Hajime J
AU  - Yuasa HJ
AD  - Molecular Immunopathology Unit, Discipline of Pathology, School of Medical 
      Sciences, University of Sydney, NSW 2006, Australia. julie@kochi-u.ac.jp
FAU - Ball, Helen J
AU  - Ball HJ
FAU - Ho, Yuen Fern
AU  - Ho YF
FAU - Austin, Christopher J D
AU  - Austin CJ
FAU - Whittington, Camilla M
AU  - Whittington CM
FAU - Belov, Katherine
AU  - Belov K
FAU - Maghzal, Ghassan J
AU  - Maghzal GJ
FAU - Jermiin, Lars S
AU  - Jermiin LS
FAU - Hunt, Nicholas H
AU  - Hunt NH
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Comp Biochem Physiol B Biochem Mol Biol
JT  - Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology
JID - 9516061
RN  - 0 (Indoleamine-Pyrrole 2,3,-Dioxygenase)
RN  - 0 (Recombinant Proteins)
RN  - 8DUH1N11BX (Tryptophan)
RN  - EC 1.13.11.11 (Tryptophan Oxygenase)
RN  - T42P99266K (Methylene Blue)
SB  - IM
MH  - Animals
MH  - Cloning, Molecular
MH  - Indoleamine-Pyrrole 2,3,-Dioxygenase/genetics/isolation & 
      purification/*metabolism
MH  - Methylene Blue/metabolism
MH  - Monodelphis/genetics/*metabolism
MH  - *Phylogeny
MH  - Platypus/genetics/*metabolism
MH  - Recombinant Proteins/isolation & purification/metabolism
MH  - Substrate Specificity
MH  - Tryptophan/metabolism
MH  - Tryptophan Oxygenase/genetics/isolation & purification/*metabolism
EDAT- 2009/04/30 09:00
MHDA- 2009/06/16 09:00
CRDT- 2009/04/30 09:00
PHST- 2009/04/30 09:00 [entrez]
PHST- 2009/04/30 09:00 [pubmed]
PHST- 2009/06/16 09:00 [medline]
PST - ppublish
SO  - Comp Biochem Physiol B Biochem Mol Biol. 2009 Jun;153(2):137-44.