The Rotational Mobility of Pyridoxamine 5-Phosphate

The technique of fluorescence polarization was used to study the degree of mobility of the cofactor pyridoxamine 5-phosphate bound to the catalytic site of the enzyme aspartate aminotransferase. While the cofactor of the phosphopyridoxamine form of the enzyme exhibits rotational mobility, the pyrido...

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Veröffentlicht in:	The Journal of biological chemistry 1970-01, Vol.245 (2), p.448-449
1. Verfasser:	Churchich, J E
Format:	Artikel
Sprache:	eng
Schlagworte:	Amines Aspartate Aminotransferases Binding Sites Electrochemistry Fluorescence Phosphoric Acids Pyridines Rotation Spectrophotometry Temperature Viscosity
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description	The technique of fluorescence polarization was used to study the degree of mobility of the cofactor pyridoxamine 5-phosphate bound to the catalytic site of the enzyme aspartate aminotransferase. While the cofactor of the phosphopyridoxamine form of the enzyme exhibits rotational mobility, the pyridoxyl 5-phosphate residues of the reduced enzyme are rigidly bound to the enzyme surface. These results have direct bearing on the question of the functional role played by pyridoxamine 5-phosphate during enzymatic transamination.
doi_str_mv	10.1016/S0021-9258(18)63411-8
format	Article
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source	MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects	Amines Aspartate Aminotransferases Binding Sites Electrochemistry Fluorescence Phosphoric Acids Pyridines Rotation Spectrophotometry Temperature Viscosity
title	The Rotational Mobility of Pyridoxamine 5-Phosphate
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