Literature summary for 2.7.1.71 extracted from

Cerasoli, E.; Kelly, S.M.; Coggins, J.R.; Boam, D.J.; Clarke, D.T.; Price, N.C.
The refolding of type II shikimate kinase from Erwinia chrysanthemi after denaturation in urea (2002), Eur. J. Biochem., 269, 2124-2132.

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General Stability

General Stability	Organism
the enzyme is fully unfolded in 4 M urea	Dickeya chrysanthemi

Organism

Organism	UniProt	Comment	Textmining
Dickeya chrysanthemi	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Dickeya chrysanthemi

Renatured (Commentary)

Renatured (Comment)	Organism
the enzyme is fully unfolded in 4 M urea. Approximately 95% of the enzyme activity can be recovered on dilution of the urea from 4 to 0.36 M. Refolding occurs in at least four kinetic phases, the slowest of which corresponds with the regain of shikimate binding and enzyme activity	Dickeya chrysanthemi

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + shikimate	-	Dickeya chrysanthemi	ADP + shikimate 3-phosphate	-	?

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Release 2023.1 (January 2023)