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Literature summary for 1.2.1.9 extracted from

  • Rahuel-Clermont, S.; Arutyunov, D.; Marchal, S.; Orlov, V.; Muronetz, V.; Branlant, G.
    Thermal destabilization of non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans upon phosphate binding in the active site (2005), J. Biol. Chem., 280, 18590-18597.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C302A compared to wild-type enzyme the amount of the thermolabile species is higher Streptococcus mutans
E268A compared to wild-type enzyme the amount of the thermolabile species is significantly lower Streptococcus mutans
N169T compared to wild-type enzyme the amount of the thermolabile species is significantly lower Streptococcus mutans
R459I compared to wild-type enzyme the amount of the thermolabile species is significantly lower Streptococcus mutans
T195G compared to wild-type enzyme the amount of the thermolabile species is similar Streptococcus mutans

Organism

Organism UniProt Comment Textmining
Streptococcus mutans
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde-3-phosphate + NADP+
-
Streptococcus mutans D-3-phosphoglycerate + NADPH
-
?

Synonyms

Synonyms Comment Organism
GAPN
-
Streptococcus mutans
non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase
-
Streptococcus mutans

Temperature Stability [┬░C]

Temperature Stability Minimum [┬░C] Temperature Stability Maximum [┬░C] Comment Organism
additional information
-
phosphate binds to the enzyme, resulting in the formation of a GAPN-phosphate binary complex characterized by a strongly decreased thermal stability, with a difference of at least 15┬░C between the maximum temperature of the thermal transition peaks, phosphate binds to the substrate C-3 subsite. Glycerol-3-phosphate has similar effects in thermal stability Streptococcus mutans

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Streptococcus mutans