Abstract：
:Directed mutagenesis has been used to study the nicotinamide subsite of the glycolytic NAD-dependent glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Residue Asn313 is involved together with the carboxyamide moiety of the nicotinamide ring in a complex network of hydrogen bonding interactions which fix the position of the pyridinium ring of NAD to which hydride transfer occurs at the C-4 position in the catalytic reaction. The asparagine side-chain has been replaced by that of the Thr and Ala residues and results in mutants with very similar properties. Both mutants show much weaker binding of NAD and lower catalytic efficiency. The mutant Asn313----Thr still exhibits strict B-stereospecificity in hydride transfer and retains the property of negative co-operativity in NAD binding. These experiments strongly suggest that the mutant enzyme undergoes the apo----holo sub-unit structural transition associated with coenzyme binding but that the nicotinamide ring is no longer as rigidly held in its pocket as in the wild type enzyme. The results shed light on the details of the molecular interactions which are responsible for negative co-operativity in this enzyme.
journal_name
Biochimiejournal_title
Biochimieauthors
Corbier C,Mougin A,Mely Y,Adolph HW,Zeppezauer M,Gerard D,Wonacott A,Branlant Gdoi
10.1016/0300-9084(90)90119-2subject
Has Abstractpub_date
1990-08-01 00:00:00pages
545-54issue
8eissn
0300-9084issn
1638-6183pii
0300-9084(90)90119-2journal_volume
72pub_type
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