Literature summary for 5.3.1.1 extracted from

Gruening, N.M.; Du, D.; Keller, M.A.; Luisi, B.F.; Ralser, M.
Inhibition of triosephosphate isomerase by phosphoenolpyruvate in the feedback-regulation of glycolysis (2014), Open biology, 4, 130232 .

Search for more literature for 5.3.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
-	Oryctolagus cuniculus
expression in Saccharomyces cerevsiae	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of TPI with bound phosphoenolpyruvate at 1.6 A resolution. Phosphoenolpyruvate is bound to the catalytic pocket of TPI and occludes substrate	Oryctolagus cuniculus

Protein Variants

Protein Variants	Comment	Organism
I170T	13% residual activity	Homo sapiens
I170V	5.9% residual activity	Homo sapiens
K13R	mutant is catalytically inactive and largely unstable	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
phosphoenolpyruvate	competitive	Homo sapiens
phosphoenolpyruvate	competitive	Oryctolagus cuniculus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.303	-	D-glyceraldehyde 3-phosphate	mutant I170T, pH not specified in the publication, temperature not specified in the publication	Homo sapiens
0.687	-	D-glyceraldehyde 3-phosphate	mutant I170V, pH not specified in the publication, temperature not specified in the publication	Homo sapiens
1.373	-	D-glyceraldehyde 3-phosphate	wild-type, pH not specified in the publication, temperature not specified in the publication	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-
Oryctolagus cuniculus	P00939	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glyceraldehyde 3-phosphate	-	Homo sapiens	dihydroxyacetone 3-phosphate	-	?

Synonyms

Synonyms	Comment	Organism
TpI	-	Homo sapiens
TpI	-	Oryctolagus cuniculus

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.2	-	phosphoenolpyruvate	mutant I170T, pH not specified in the publication, temperature not specified in the publication	Homo sapiens
0.23	-	phosphoenolpyruvate	wild-type, pH not specified in the publication, temperature not specified in the publication	Homo sapiens
0.5	-	phosphoenolpyruvate	mutant I170V, pH not specified in the publication, temperature not specified in the publication	Homo sapiens

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.154	-	mutant I170T, pH not specified in the publication, temperature not specified in the publication	Homo sapiens	phosphoenolpyruvate
0.193	-	mutant I170V, pH not specified in the publication, temperature not specified in the publication	Homo sapiens	phosphoenolpyruvate
0.57	-	wild-type, pH not specified in the publication, temperature not specified in the publication	Homo sapiens	phosphoenolpyruvate

General Information

General Information	Comment	Organism
physiological function	glycolytic regulation requires direct catalytic inhibition of TPI by the pyruvate kinase substrate phosphoenolpyruvate	Oryctolagus cuniculus
physiological function	transgenic yeast cells expressing mutations I170V or I170T accumulate greater levels of pentose phosphate pathway intermediates and have altered stress resistance, mimicking the activation of the pyruvate kinase-TPI feedback loop. Glycolytic regulation requires direct catalytic inhibition of TPI by the pyruvate kinase substrate phosphoenolpyruvate	Homo sapiens

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Release 2023.1 (January 2023)