The regulatory center of D-glyceraldehyde-3-phosphate dehydrogenase

Ovádi, Judit and Nuridsány, Mimi and Keleti, Tamás (1972) The regulatory center of D-glyceraldehyde-3-phosphate dehydrogenase. ACTA BIOCHIMICA ET BIOPHYSICA ACADEMIAE SCIENTIARUM HUNGARICAE, 7. pp. 133-141. ISSN 0001-5253

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Abstract

Glyceraldehyde-3-phosphate dehydrogenase containing bound NAD is unable to bind tightly ATP. The enzyme-ATP complex can bind firmly only two moles of NAD with concomitant weakening of the enzyme-ATP binding. The enzyme containing bound ATP forms completely the enzyme-NAD charge-transfer complex. Accordingly, ATP is not bound at the NAD-binding site in the active center. The binding of adenosine phosphates (ATP, ADP, AMP) suspends the inhibi tion of enzymatic activity by excess NAD or inorganic phosphate. Adenine and ade nosine affect only the inhibition by excess NAD. We suggest that apart from the active site each subunit of glyceraldehyde-3-phosphate dehydrogenase has a specific regulatory site. Binding of NAD, adenosine phosphates or inorganic phosphate to this site decreases enzymatic activity.

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