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Literature summary for 1.2.1.12 extracted from

  • Markossian, K.A.; Golub, N.V.; Chebotareva, N.A.; Asryants, R.A.; Naletova, I.N.; Muronetz, V.I.; Muranov, K.O.; Kurganov, B.I.
    Comparative analysis of the effects of alpha-crystallin and GroEL on the kinetics of thermal aggregation of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (2010), Protein J., 29, 11-25.
    View publication on PubMed

General Stability

General Stability Organism
alpha-crystallin accelerates the thermal inactivation of GAPDH, while GroEL does not affect thermal inactivation and denaturation of GAPDH Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homotetramer
-
Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
GAPDH
-
Oryctolagus cuniculus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
45
-
GAPDH is inactivated at 45°C, alpha-crystallin accelerates the thermal inactivation of GAPDH at 45°C and reduces thermostability of the enzyme, while GroEL does not affect thermal inactivation and denaturation of GAPDH Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Oryctolagus cuniculus