Autor:	Natalia K. Nagradova
Rok vydání:	2001
Předmět:	chemistry.chemical_classification biology Stereochemistry Cooperative binding Dehydrogenase General Medicine Biochemistry Active center Enzyme stomatognathic system chemistry Tetramer biology.protein NAD+ kinase Binding site Glyceraldehyde 3-phosphate dehydrogenase
Zdroj:	Biochemistry (Moscow). 66:1067-1076
ISSN:	0006-2979
DOI:	10.1023/a:1012472627801
Popis:	The properties of the active center of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are considered with emphasis on the structure of anion-binding sites and their role in catalysis. The results of studies on the molecular mechanism of the effect of NAD+ on the enzyme conformation are discussed. Experimental evidence is presented supporting the idea that negative cooperativity of NAD+ binding and half-of-the-sites reactivity exhibited by GAPDH are generated by different mechanisms. Data obtained with rabbit muscle and Escherichia coli GAPDH point to preexisting asymmetry in these tetramers. Structural determinants that can control the transition of the tetramer from the symmetric to the asymmetric state were found.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::7e566607ae8232445f1804dfa07d2a8e https://doi.org/10.1023/a:1012472627801 Zobrazit plný text záznamu Full text from SpringerLink