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.

Search for more literature for 1.2.1.9

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

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Release 2023.1 (January 2023)