1-l-methyltryptophan is a more effective inhibitor of vertebrate IDO2 enzymes than 1-d-methyltryptophan

Journal article


Yuasa, Hajime J., Ball, Helen J., Austin, Christopher J. D. and Hunt, Nicholas H.. (2010). 1-l-methyltryptophan is a more effective inhibitor of vertebrate IDO2 enzymes than 1-d-methyltryptophan. Comparative Biochemistry and Physiology B: Biochemistry and Molecular Biology. 157(1), pp. 10 - 15. https://doi.org/10.1016/j.cbpb.2010.04.006
AuthorsYuasa, Hajime J., Ball, Helen J., Austin, Christopher J. D. and Hunt, Nicholas H.
Abstract

1-d-methyltryptophan (D-1MT) is an effective anti-cancer agent in mouse tumour models. It has been suggested to be a selective inhibitor of the recently described tryptophan-degrading enzyme indoleamine 2,3-dioxygenase 2 (IDO2) rather than the closely related enzyme IDO1. We found that mammalian (mouse, opossum and platypus), chicken, frog, and fish IDO2 could be functional tryptophan-catabolising enzymes. The characteristics of pH-dependent activity and inhibitor selectivity were conserved amongst the vertebrate IDO2 proteins tested. Like IDO1 enzymes, the enzymatic activity of all IDO2s was inhibited by L-1MT but not by D-1MT in a cell-free assay. When IDO2s were expressed in mammalian cells, L-1MT was also a better inhibitor than D-1MT.

Keywordsindoleamine 2; 3-dioxygenase 2; inhibitor selectivity; substrate specificity; tryptophan degradation
Year2010
JournalComparative Biochemistry and Physiology B: Biochemistry and Molecular Biology
Journal citation157 (1), pp. 10 - 15
PublisherElsevier Science
ISSN1096-4959
Digital Object Identifier (DOI)https://doi.org/10.1016/j.cbpb.2010.04.006
Scopus EID2-s2.0-77954143054
Page range10 - 15
Research GroupSchool of Behavioural and Health Sciences
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File Access Level
Controlled
Place of publicationUnited States of America
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