Application | Comment | Organism |
---|---|---|
drug development | GAPDH is an important drug target | Bos taurus |
Crystallization (Comment) | Organism |
---|---|
purified native tetrameric enzyme with either three or four bound NAD+ molecules, bGAPDH can be crystallized directly from isotonic extracts of ROS, X-ray diffraction structure determination and analysis at 1.93 A and 1.54 A resolution, respectively, molecular replacement using the coordinates of one monomer of rabbit-muscle GAPDH, PDB ID 1J0X, without ligand and water to search the initial model, modelling | Bos taurus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.153 | - |
D-glyceraldehyde 3-phosphate | pH and temperature not specified in the publication | Bos taurus | |
0.255 | - |
NAD+ | pH and temperature not specified in the publication | Bos taurus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
150000 | - |
gel filtration | Bos taurus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Bos taurus | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bos taurus | Q2KJE5 | - |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from bovine retinas using NAD+-agarose affinity chromatography | Bos taurus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
eye | - |
Bos taurus | - |
photoreceptor | - |
Bos taurus | - |
retina | - |
Bos taurus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Bos taurus | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | 4 * 36000, SDS-PAGE | Bos taurus |
More | structure analysis, overview. Dual side-chain conformations are observed in Ser207 in subunits of O, Q, and R of the bGAPDH(NAD)3 | Bos taurus |
Synonyms | Comment | Organism |
---|---|---|
GAPDH | - |
Bos taurus |
glyceraldehyde-3-phosphate dehydrogenase | - |
Bos taurus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | differing occupancy by NAD, bGAPDH(NAD)4, and bGAPDH(NAD)3 in the homotetramer, structure analysis, overview. Importance of Phe34 in NAD+ binding, Phe34 is stabilized in the presence of NAD+ but displays greater mobility in its absence. The oxidative state of the active site Cys149 residue is regulated by NAD+ binding, because this residue is found oxidized in the absence of dinucleotide. The distance between Cys149 and His176 decreases upon NAD binding and Cys149 remains in a reduced state when NAD+ is bound. Dual side-chain conformations are observed in Ser207 in subunits of O, Q, and R of the bGAPDH(NAD)3. Residues Pro33 and Phe34 form a bottleneck for NAD+ binding | Bos taurus |
General Information | Comment | Organism |
---|---|---|
malfunction | substitution of Phe34 with smaller side chain (e.g. Gly or Leu), or polar residue (e.g. Thr) abolishes the NAD+ binding affinity, or reduce the protein's catalytic efficiency | Bos taurus |
additional information | importance of Phe34 in NAD+ binding, Phe34 is stabilized in the presence of NAD+ but displays greater mobility in its absence. The oxidative state of the active site Cys149 residue is regulated by NAD+ binding, because this residue is found oxidized in the absence of dinucleotide. The distance between Cys149 and His176 decreases upon NAD binding and Cys149 remains in a reduced state when NAD+ is bound, cofactor binding and active site structures, catalytic mechanism, overview | Bos taurus |
physiological function | the enzyme plays a central role in glycolysis, and nonglycolytic processes such as nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis | Bos taurus |