Literature summary for 5.1.3.3 extracted from

Beebe, J.A.; Arabshahi, A.; Clifton, J.G.; Ringe, D.; Petsko, G.A.; Frey, P.A.
Galactose mutarotase: pH dependence of enzymatic mutarotation (2003), Biochemistry, 42, 4414-4420.

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KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
4	-	alpha-D-galactose	pH 7.0, 25°C	Escherichia coli
38	-	alpha-D-glucose	pH 7.0, 25°C	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A9C3	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
alpha-D-glucose = beta-D-glucose	mechanism, one of the catalytic groups H104, H175, or E309, shuttles a proton to and from the endocyclic oxygen and the other two shuttle protons to the anomeric oxygen atoms. Ring opening of alpha-D-glucose limits the rate at low pH, but ring closure does not become rate limiting at pH up to 8.5	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
alpha-D-galactose	-	Escherichia coli	beta-D-galactose	-	?
alpha-D-glucose	-	Escherichia coli	beta-D-glucose	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	turnover number is not dependent on pH-value	Escherichia coli
18400	-	alpha-D-galactose	pH 7.0, 25°C	Escherichia coli
19000	-	alpha-D-glucose	pH 7.0, 25°C	Escherichia coli

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Release 2023.1 (January 2023)