Literature summary for 3.2.1.23 extracted from

Kappelhoff, J.C.; Liu, S.Y.; Dugdale, M.L.; Dymianiw, D.L.; Linton, L.R.; Huber, R.E.
Practical considerations when using temperature to obtain rate constants and activation thermodynamics of enzymes with two catalytic steps: native and N460T-beta-alactosidase (E. coli) as Examples (2009), Protein J., 28, 96-103.

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Protein Variants

Protein Variants	Comment	Organism
N460T	analysis of rate constants and activation thermodynamics to demonstrate the valuable mechanistic details of enzymes that can be obtained from studies of this type	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	discussion of precautions and recommendations for measuring values of the rate constants and the associated enthalpies and entropies of enzymes with two catalytic steps by determining the effects of temperature on the kcat values	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P00722	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2-nitrophenyl beta-D-galactopyranoside + H2O	-	Escherichia coli	2-nitrophenol + D-galactose	-	?
4-nitrophenyl beta-D-galactopyranoside + H2O	-	Escherichia coli	4-nitrophenol + D-galactose	-	?

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Release 2023.1 (January 2023)