Glyceraldehyde 3-phosphate dehydrogenase

GAPDH
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesGAPDH, GAPD, G3PD, HEL-S-162eP, glyceraldehyde-3-phosphate dehydrogenase
External IDsOMIM: 138400; MGI: 5434255; HomoloGene: 107053; GeneCards: GAPDH; OMA:GAPDH - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

XM_001476707

RefSeq (protein)

NP_001243728
NP_001276674
NP_001276675
NP_002037
NP_001344872

NP_001276655
NP_032110

Location (UCSC)Chr 12: 6.53 – 6.54 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
determinants of enzyme thermostability observed in the molecular structure of thermus aquaticus d-glyceraldehyde-3-phosphate dehydrogenase at 2.5 angstroms resolution
Identifiers
SymbolGp_dh_N
PfamPF00044
Pfam clanCL0063
InterProIPR020828
PROSITEPDOC00069
SCOP21gd1 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain
crystal structure of glyceraldehyde-3-phosphate dehydrogenase from pyrococcus horikoshii ot3
Identifiers
SymbolGp_dh_C
PfamPF02800
Pfam clanCL0139
InterProIPR020829
PROSITEPDOC00069
SCOP21gd1 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Glyceraldehyde 3-phosphate dehydrogenase (abbreviated GAPDH) (EC 1.2.1.12) is an enzyme of about 37kDa that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In addition to this long established metabolic function, GAPDH has recently been implicated in several non-metabolic processes, including transcription activation, initiation of apoptosis,[4] ER-to-Golgi vesicle shuttling, and fast axonal, or axoplasmic transport.[5] In sperm, a testis-specific isoenzyme GAPDHS is expressed.

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000111640Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Tarze A, Deniaud A, Le Bras M, Maillier E, Molle D, Larochette N, Zamzami N, Jan G, Kroemer G, Brenner C (April 2007). "GAPDH, a novel regulator of the pro-apoptotic mitochondrial membrane permeabilization". Oncogene. 26 (18): 2606–2620. doi:10.1038/sj.onc.1210074. PMID 17072346. S2CID 20291542.
  5. ^ Zala D, Hinckelmann MV, Yu H, Lyra da Cunha MM, Liot G, Cordelières FP, Marco S, Saudou F (January 2013). "Vesicular glycolysis provides on-board energy for fast axonal transport". Cell. 152 (3): 479–491. doi:10.1016/j.cell.2012.12.029. PMID 23374344.