Literature summary for 2.7.1.71 extracted from

Cerasoli, E.; Kelly, S.M.; Coggins, J.R.; Lapthorn, A.J.; Clarke, D.T.; Price, N.C.
Effects of salts on the function and conformational stability of shikimate kinase (2003), Biochim. Biophys. Acta, 1648, 43-54.

Organism

Organism	UniProt	Comment	Textmining
Dickeya chrysanthemi	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
when the enzyme is unfolded by incubation in 4 M urea, addition of NaCl or Na2SO4 leads to relatively slow refolding of the enzyme. The refolded enzyme can bind shikimate, though more weakly than the native enzyme. The refolded enzyme does not appear to be capable of binding nucleotides, nor does it possess detectable catalytic activity. The refolding process brought about by addition of salt in the presence of 4 M urea is not associated with any change in the fluorescence of the probe 8-anilino-1-naphthalenesulfonic acid	Dickeya chrysanthemi

Renatured (Comment)

Organism

when the enzyme is unfolded by incubation in 4 M urea, addition of NaCl or Na2SO4 leads to relatively slow refolding of the enzyme. The refolded enzyme can bind shikimate, though more weakly than the native enzyme. The refolded enzyme does not appear to be capable of binding nucleotides, nor does it possess detectable catalytic activity. The refolding process brought about by addition of salt in the presence of 4 M urea is not associated with any change in the fluorescence of the probe 8-anilino-1-naphthalenesulfonic acid

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)