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Ornithine Aminotransferase versus GABA Aminotransferase: Implications for the Design of New Anticancer Drugs
Author(s) -
Lee Hyunbeom,
Juncosa Jose I.,
Silverman Richard B.
Publication year - 2015
Publication title -
medicinal research reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.868
H-Index - 130
eISSN - 1098-1128
pISSN - 0198-6325
DOI - 10.1002/med.21328
Subject(s) - ornithine aminotransferase , enzyme , biochemistry , chemistry , small molecule , ornithine , pharmacology , biology , amino acid , arginine
Ornithine aminotransferase (OAT) and γ‐aminobutyric acid aminotransferase (GABA‐AT) are classified under the same evolutionary subgroup and share a large portion of structural, functional, and mechanistic features. Therefore, it is not surprising that many molecules that bind to GABA‐AT also bind well to OAT. Unlike GABA‐AT, OAT had not been viewed as a potential therapeutic target until recently; consequently, the number of therapeutically viable molecules that target OAT is very limited. In this review the two enzymes are compared with respect to their active‐site structures, catalytic and inactivation mechanisms, and selective inhibitors. Insight is offered that could aid in the design and development of new selective inhibitors of OAT for the treatment of cancer.