Literature summary for 5.3.1.9 extracted from

Repiso, A.; Oliva, B.; Vives Corrons, J.L.; Carreras, J.; Climent, F.
Glucose phosphate isomerase deficiency: enzymatic and familial characterization of Arg346His mutation (2005), Biochim. Biophys. Acta, 1740, 467-471.

Search for more literature for 5.3.1.9

Application

Application	Comment	Organism
medicine	mutation A346H is identified in a patient suffering fromchronic nonspherocytic hemolytic anemia. Mutation results in loss of 82% of enzyme activity, loss of enzyme capability to dimerize, and in significant changes in erythrocyte metabolism	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
A346H	mutation identified in a patient suffering from chronic nonspherocytic hemolytic anemia. Loss of 82% of enzyme activity, loss of enzyme capability to dimerize. Mutation results in significant changes in erythrocyte metabolism	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
169	-	D-fructose 6-phosphate	wild-type, 37°C, pH 8.0	Homo sapiens
170	-	D-fructose 6-phosphate	mutant A346H, 37°C, pH 8.0	Homo sapiens
221	-	D-glucose 6-phosphate	wild-type, 37°C, pH 8.0	Homo sapiens
267.4	-	D-glucose 6-phosphate	mutant A346H, 37°C, pH 8.0	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	patient suffering chronic nonspherocytic hemolytic anemia	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-fructose 6-phosphate	-	Homo sapiens	D-glucose 6-phosphate	-	r
D-glucose 6-phosphate	-	Homo sapiens	D-fructose 6-phosphate	-	r

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)