Glyceraldehyde-3-phosphate dehydrogenase (Mus musculus)

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Basic Information
Short Name Gapdh
UNP ID P16858
Organism Mus musculus
Cys Site Cys154
Family/Domain Glyceraldehyde-3-phosphate dehydrogenase family
Known Ligand Ligand list
Function Type Metabolic enzyme

Summary

Protein Function

Under normal cellular conditions, cytoplasmic GAPDH exists primarily as a tetramer. This form is composed of four identical 37-kDa subunits containing a single catalytic thiol group each and critical to the enzyme's catalytic function. Nuclear GAPDH has increased isoelectric point (pI) of pH 8.3–8.7. Of note, the cysteine residue Cys152 in human GAPDH's (Cys154 in mouse) active site is required for the induction of apoptosis by oxidative stress. Notably, post-translational modifications of cytoplasmic GAPDH contribute to its functions outside of glycolysis. (From Wikipedia)

566-function.png
The reaction of GAPDH catalyzed

Cys Function & Property

Cys154 is the active site and very close to one of the Glyceraldehyde 3-phosphate binding sites of GAPDH, residues 149-151.

  • Hydrophobic property:
566-hydro.png
  • SASA:
Cys154: Unknown

Protein Sequence

MVKVGVNGFG RIGRLVTRAA ICSGKVEIVA INDPFIDLNY MVYMFQYDST
HGKFNGTVKA ENGKLVINGK PITIFQERDP TNIKWGEAGA EYVVESTGVF
TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLKIVSNASC
TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA
AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP
AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA
LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE

Structural Information

  • Known structure with covalent ligand:
Unknown
  • Protein structure:
Unknown

Related Pathway

Experimental Evidence

UPLC-MS, Two-dimensional SDS–PAGE

Reference

  1. Miura T, Shinkai Y, Hirose R, et al. Glyceraldehyde-3-phosphate dehydrogenase as a quinone reductase in the suppression of 1, 2-naphthoquinone protein adduct formation[J]. Free Radical Biology and Medicine, 2011, 51(11): 2082-2089. 21963991