EC Number   |
General Information |
Reference |
|---|
    1.2.1.12 | evolution |
both GAPDS and GAPD are homotetramers with the sequence identity of about 70%. They are encoded by different genes which have emerged after duplication of the original gene during the early evolution of chordates |
741963 |
| 1.2.1.12 | evolution |
both GAPDS and GAPD are homotetramers with the sequence identity of about 70%. They are encoded by different genes which have emerged after duplication of the original gene during the early evolution of chordates. The GAPDS gene is lost by most lineages, and specialized to a testis-specific protein in reptilians and mammals |
741963 |
| 1.2.1.12 | evolution |
cellular glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a phylogenetically conserved, ubiquitous enzyme |
743173 |
| 1.2.1.12 | evolution |
convergent evolution in GapA/B and GapC1, plastid GapC1 and GapA represent two independent cases of functional divergence and adaptations to the Calvin cycle entailing a shift in subcellular targeting and a shift in binding preference from NAD+ to NADPH. Comparisons between GapA sequences and cytosolic GAPDH and GapC1 and cytosolic GAPDH sequences (Gap2, GapA, GapB, or GapC1) to identify possible functionally divergent sites, homology modeling, phylogenetic tree, detailed overview |
743636 |
| 1.2.1.12 | evolution |
molecular phylogenetic tree using sequences from 26 GAPDH proteins from 12 species of Aspergillus and 8 species of Trichoderma genus |
-, 762945 |
| 1.2.1.12 | evolution |
sequence comparisons |
-, 762770 |
| 1.2.1.12 | evolution |
the sequence of the isozyme uracil-DNA glycosylase, UDG polypeptide (331 amino acids), differs from the sequence of classical GAPDH (335 amino acids) by the substitution of the residues 194-213 and the deletion of the residues 328-330. The amino acid sequence of the GAPDH isoform UDG because of its activity is hardly connected with alternative splicing of GAPDH pre-mRNA. The UDG region with the altered amino acids 194-213 is situated within the exon far from its boundaries. It appears to be a result of the single-nucleotide deletion in the GAPDH gene exon, causing the shift of the reading frame. Downstream to this region, there is theadditional deletion of 2 nucleotides in the UDG sequence, leading to restoration of the initial reading frame. The observed discrepancies in the sequences of these proteins are likely due to a sequencing error. Interestingly, the altered region belongs to the GAPDH glyceraldehyde-3-phosphate-binding site not participating in DNA binding |
743329 |
| 1.2.1.12 | malfunction |
FAO hepatoma cells with mutations of all 4 lysine residues (4K-R-GAPDH) in critical regions of enzyme GAPDH to mimic their unmodified state show reduced GAPDH glycolytic activity and glycolytic flux and increased gluconeogenic GAPDH activity and glucose production. Hepatic expression of mutant 4K-R-GAPDH in mice increases GAPDH gluconeogenic activity and the contribution of gluconeogenesis to endogenous glucose production in the unfed state. Consistent with the increased reliance on the energy-consuming gluconeogenic pathway, plasma free fatty acids and ketones are elevated inmice expressing 4K-RGAPDH, suggesting enhanced lipolysis and hepatic fatty acid oxidation. GAPDH acetylation is reduced in obese and type 2 diabetic db/db mice |
-, 742477 |
| 1.2.1.12 | malfunction |
GAPDH knockdown abolishes cADPR-induced Ca2+ release. GAPDH knockdown markedly inhibits NPE-cADPR- or PALcIDPRE-induced cytosolic Ca2+ increase in Jurkat cells, RyR3-expressing HEK-293 cells, or human coronary artery smooth muscle cells. Washing saponin-treated cells with PBS abolishes cADPR-induced colocalization of GAPDH with ryanodine receptors, RyRs |
742751 |
| 1.2.1.12 | malfunction |
GAPDH-deficient cells are more sensitive to bleomycin or methyl methanesulfonate. In cells challenged with these genotoxic agents, GAPDH deficiency results in reduced cell viability and filamentous growth |
742668 |
