D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE - PREEXISTENT ASYMMETRY OFTHE TETRAMER AND ITS FUNCTIONAL IMPLICATIONS

Citation
Nk. Nagradova et al., D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE - PREEXISTENT ASYMMETRY OFTHE TETRAMER AND ITS FUNCTIONAL IMPLICATIONS, Biotechnology and applied biochemistry, 18, 1993, pp. 157-163
Citations number
16
Categorie Soggetti
Biology,"Biothechnology & Applied Migrobiology
ISSN journal
08854513
Volume
18
Year of publication
1993
Part
2
Pages
157 - 163
Database
ISI
SICI code
0885-4513(1993)18:<157:DD-PAO>2.0.ZU;2-Y
Abstract
Modification of a single arginine residue per subunit of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase stabilizes the tetramer in a conformation wherein only two active sites are capable of performin g catalysis (oxidation Of D-glyceraldehyde 3-phosphate or hydrolysis o f p-nitrophenyl acetate). The modified enzyme exhibits half-of-the-sit es reactivity towards iodoacetate and iodoacetamide, known to be 'all- of-the-sites reagents' with the native enzyme. Evidence is presented s upporting the model of a built-in asymmetry of the tetramer. The resul ts obtained suggest that the arginine residue (probably Arg-231) contr ols the conformational transition between the asymmetric and symmetric states of the tetramer.