Glutamate dehydrogenase from two Antarctic organisms, the icefishChaenocephalus aceratusand the bacteriumPsychrobactersp. TAD1

Autor:	Antonella Antignani, Vito Carratore, Raffaela Di Fraia, Laura Camardella, Guido di Prisco, M. Antonietta Ciardiello
Rok vydání:	2000
Předmět:	chemistry.chemical_classification biology Cold adaptation Glutamate dehydrogenase Hydrostatic pressure Chaenocephalus aceratus Pressure adaptation Notothenioidei biology.organism_classification Channichthyidae Enzyme chemistry Biochemistry Antarctica Animal Science and Zoology NAD+ kinase Bacteria
Zdroj:	Bollettino di zoologia 67 (2000): 27–32. doi:10.1080/11250000009356352 info:cnr-pdr/source/autori:Ciardiello MA, Di Fraia R, Antignani A, Carratore V, Camardella L di Prisco G./titolo:Glutamate dehydrogenase from two Antarctic organisms, the icefish Chaenocephalus aceratus and the bacterium Psychrobacter sp. TAD1./doi:10.1080%2F11250000009356352/rivista:Bollettino di zoologia/anno:2000/pagina_da:27/pagina_a:32/intervallo_pagine:27–32/volume:67
ISSN:	1748-5851 1125-0003
DOI:	10.1080/11250000009356352
Popis:	Glutamate dehydrogenase (GDH) was purified from the liver of the teleost Chaenocephalus aceratus (Notothenioidei: Channichthyidae) and the microorganism Psychrobacter sp. TAD1, from Antarctic marine and terrestrial environments, respectively. GDH isolated from C. aceratus liver had a hexameric molecular structure very similar to that of other vertebrates and displayed preference for NAD+, a feature shared with other fish enzymes. The bovine and fish GDH activity and stability were differently affected by temperature and hydrostatic pressure. At low temperatures, the specific activity of fish GDH was higher than that measured with the homologous bovine enzyme. Psychrobacter sp. TAD1 showed a feature quite unusual in bacteria, i.e. the presence of two distinct GDHs specific either for NADP+ or for NAD+. NADP+ -dependent GDH was purified and characterised. It has a hexameric structure with a subunit molecular weight similar to that described for this class of GDHs and a specific activity at low and moderate temperatures similar to that measured with the homologous enzyme from Escherichia coli. The kinetic properties of NADP+ -dependent GDH of Psychrobacter sp. TAD1 and the presence of another NAD+-dependent GDH suggest that, during the cold-adaptation process, this enzymatic function acquired a pattern of changes different from that of C. aceratus.
Databáze:	OpenAIRE
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