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Literature summary for 1.2.1.12 extracted from

  • Kishimoto, N.; Onitsuka-Kishimoto, A.; Iga, N.; Takamune, N.; Shoji, S.; Misumi, S.
    The C-terminal domain of glyceraldehyde 3-phosphate dehydrogenase plays an important role in suppression of tRNALys3 packaging into human immunodeficiency virus type-1 particles (2016), Biochem. Biophys. Rep., 8, 325-332 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of wild-type and mutant enzymes in HEK-293 cells Homo sapiens

Protein Variants

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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Homo sapiens
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3-phospho-D-glyceroyl phosphate + NADH + H+
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens P04406
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
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Homo sapiens 3-phospho-D-glyceroyl phosphate + NADH + H+
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?

Subunits

Subunits Comment Organism
homotetramer
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Homo sapiens
More molecular docking simulation Homo sapiens

Synonyms

Synonyms Comment Organism
glyceraldehyde 3-phosphate dehydrogenase
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Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
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Homo sapiens

General Information

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