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Multiple Forms of Glutamate Dehydrogenase in Animals: Structural Determinants and Physiological Implicationsстатья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 25 апреля 2017 г.
- Авторы: Bunik Victoria, Artiukhov Artem, Aleshin Vasily, Mkrtchyan Garik
- Журнал: Biology
- Том: 5
- Номер: 4
- Год издания: 2016
- Издательство: MDPI Publishing
- Местоположение издательства: Basel, Switzerland, Switzerland
- Первая страница: 1
- Последняя страница: 30
- Номер статьи: 53
- DOI: 10.3390/biology5040053
- Аннотация: Glutamate dehydrogenase (GDH) of animal cells is usually considered to be a mitochondrial enzyme. However, this enzyme has recently been reported to be also present in nucleus, endoplasmic reticulum and lysosomes. These extramitochondrial localizations are associated with moonlighting functions of GDH, which include acting as a serine protease or an ATP-dependent tubulin-binding protein. Here, we review the published data on kinetics and localization of multiple forms of animal GDH taking into account the splice variants, post-translational modifications and GDH isoenzymes, found in humans and apes. The kinetic properties of human GLUD1 and GLUD2 isoenzymes are shown to be similar to those published for GDH1 and GDH2 from bovine brain. Increased functional diversity and specific regulation of GDH isoforms due to alternative splicing and post-translational modifications are also considered. In particular, these structural differences may affect the well-known regulation of GDH by nucleotides which is related to recent identification of thiamine derivatives as novel GDH modulators. The thiamine-dependent regulation of GDH is in good agreement with the fact that the non-coenzyme forms of thiamine, i.e., thiamine triphosphate and its adenylated form are generated in response to amino acid and carbon starvation.
- Добавил в систему: Мкртчян Гарик Варданович