Cloned (Comment) | Organism |
---|---|
recombinant expression of wild-type and mutant enzymes in HEK-293 cells | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
D256R/K260E | site-directed mutagenesis, the double mutation of GAPDH results in loss of detectable binding activity to wild-type capsid N-terminal domain | Homo sapiens |
D256R/K260E/K263E/E267R | site-directed mutagenesis, multiple-substituted GAPDH mutant D256R/K260E/K263E/E267R retains the oligomeric formation with wild-type GAPDH in HIV-1 producing cells, but the incorporation level of the hetero-oligomer is decreased in viral particles. The viruses produced from cells expressing the D256R/K260E/K263E/E267R mutant restores tRNALys3 packaging efficiency because the mutant exerts a dominant negative effect by preventing wild-type GAPDH from binding to matrix region and capsid N-terminal domain and improves the reverse transcription | Homo sapiens |
D256R/K260E/Q264A | site-directed mutagenesis, the mutant lacks the ability to bind to the wild-type capsid N-terminal domain | Homo sapiens |
D256R/K260E/Q264A/E267R | site-directed mutagenesis, the mutant lacks the binding ability to the wild-type capsid N-terminal domain | Homo sapiens |
D356R | site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region | Homo sapiens |
E267R | site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region | Homo sapiens |
K263E | site-directed mutagenesis, the mutation leads to loss of the ability to bind to wild-type matrix region | Homo sapiens |
additional information | viral mutations R58E, Q59A or Q63A in the matrix region, and E76R or R82E in the capsid N-terminal domain abrogate the interaction with the C-terminal domain of enzyme GAPDH. SAccharomyces cerevisiae two-hydrib interaction analysis between enzyme GAPDH wild-type and mutants with HIV-1 wild-type and mutant matrix region and capsid N-terminal domain, overview | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Homo sapiens | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P04406 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Homo sapiens | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
homotetramer | - |
Homo sapiens |
More | molecular docking simulation | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
glyceraldehyde 3-phosphate dehydrogenase | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | molecular docking simulation | Homo sapiens |
physiological function | the C-terminal domain of human host cell glyceraldehyde 3-phosphate dehydrogenase plays an important role in suppression of tRNALys3 packaging into human immunodeficiency virus type-1 particles. Human immunodeficiency virus type-1 (HIV-1) requires the packaging of human tRNALys3 as a primer for effective viral reverse transcription. The binding of human GAPDH to Pr55gag is important for the suppression mechanism, and residues Asp256, Lys260, Lys263 and Glu267 of GAPDH are essential for the suppression of tRNALys3 packaging. The C-terminal domain of GAPDH (151-335) interacts with both the matrix region (MA, 1-132) and capsid N-terminal domain (CANTD, 133-282) | Homo sapiens |