Literature summary for 3.5.1.14 extracted from

Kim, S.H.; Zhang, J.; Jiang, Y.; Zhou, H.M.; Yan, Y.B.
Assisting the reactivation of guanidine hydrochloride-denatured aminoacylase by hydroxypropyl cyclodextrins (2006), Biophys. J., 91, 686-693.

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
native enzyme from kidney by acetone precipitation, ion exchange chromatography, and gel filtration	Sus scrofa

Renatured (Commentary)

Renatured (Comment)	Organism
assisting the reactivation of guanidine hydrochloride-denatured aminoacylase by hydroxypropyl cyclodextrins in a concentration-dependent manner, most efficiently by hydroxypropyl beta-cyclodextrin, low concentrations of hydroxypropyl alpha-cyclodextrin and high concentrations of hydroxypropyl gamma-cyclodextrin promoted off-pathway aggregation, recovery of secondary and tertiary structures, overview	Sus scrofa

Renatured (Comment)

Organism

assisting the reactivation of guanidine hydrochloride-denatured aminoacylase by hydroxypropyl cyclodextrins in a concentration-dependent manner, most efficiently by hydroxypropyl beta-cyclodextrin, low concentrations of hydroxypropyl alpha-cyclodextrin and high concentrations of hydroxypropyl gamma-cyclodextrin promoted off-pathway aggregation, recovery of secondary and tertiary structures, overview

Sus scrofa

Source Tissue

Source Tissue	Comment	Organism	Textmining
kidney	-	Sus scrofa	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
chloroacetyl-L-leucine + H2O	-	Sus scrofa	chloroacetate + L-leucine	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Sus scrofa

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Release 2023.1 (January 2023)