Crystallization (Comment) | Organism |
---|---|
purified apo-form GAPDH3, by vapor-diffusing method, mixing 10 mg/mL protein with a reservoir solution containing 12% (w/v) PEG 3350, 0.1 M sodium malonate, pH 4.0, 2 days, at 14°C, X-ray diffraction structure determination and analysis at 2.49 A resolution, modeling | Saccharomyces cerevisiae |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NAD+ | NAD+ inhibition for GAPDH3 RNA binding capability, NAD+ inhibits the AUUUA binding. The inhibition effect is weaker for the 5-base substrate than for the 13-base substrate. RNA substrate binding needs to competitively displace the NAD+ molecules from the binding groove | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Saccharomyces cerevisiae | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P00359 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Saccharomyces cerevisiae | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | SDS-PAGE and gel filtration | Saccharomyces cerevisiae |
More | quarternary structure analysis and comparisons, overview | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
GAPDH | - |
Saccharomyces cerevisiae |
GAPDH3 | - |
Saccharomyces cerevisiae |
glyceraldehyde-3-phosphate dehydrogenase | - |
Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.6 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | binding structure analysis: the NAD+ molecule inserts its pyrimidine ring into a narrow hydrophobic binding pocket on the positively charged surface of GAPDH3. The residues Asn7, Gly8, Phe9, Gly10, Asp33, Pro34, Phe35, The97, Gly98, and Phe100 tightly enclose the pyrimidine ring of NAD+. Because of a common adenine head, adenosine can also bind tightly to this hydrophobic binding pocket. There are two consecutive positively charged regions that contain an NAD+-binding site, one of which is located on each side of the tetramer | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
physiological function | glyceraldehyde-3-phosphate dehydrogenase is an essential enzyme in the glycolytic pathway. GAPDH also displays a range of other functions unrelated to its glycolytic function. GAPDH is a 3'-AU-rich element-binding protein, it can selectively bind to AU-rich +element, RNA recognition mechanism, overview. NAD1 inhibition for GAPDH3 RNA binding capability indicates that GAPDH3 likely binds to the AU-rich or polyadenosine RNA substrates through its NAD+-binding domain in vitro | Saccharomyces cerevisiae |