Literature summary for 4.2.1.10 extracted from

Price, N.C.; Boam, D.J.; Kelly, S.M.; Duncan, D.; Krell, T.; Gourley, D.G.; Coggins, J.R.; Virden, R.; Hawkins, A.R.
The folding and assembly of the dodecameric type II dehydroquinases (1999), Biochem. J., 338, 195-202.

No PubMed abstract available

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-
Streptomyces coelicolor	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
at 0.5 mM guanidinium chloride the enzyme dissociates into trimeric units with little or no change in the secondary or tertiary structure and a 15% loss of activity. At higher concentrations the enzyme undergoes sharp unfolding transitions. When the concentration is lowered from 6M to 0.55 M the enzyme refolds in an efficient manner to form trimeric units with more than 75% regain of activity	Streptomyces coelicolor
at 0.5 mM guanidinium chloride the enzyme dissociates into trimeric units with little or no change in the secondary or tertiary structure and a 55% increase of activity. At higher concentrations the enzyme undergoes sharp unfolding transitions. When the concentration is lowered from 6 M to 0.55 M the enzyme refolds in an efficient manner to form trimeric units with less than 35% regain of activity	Mycobacterium tuberculosis

Renatured (Comment)

Organism

at 0.5 mM guanidinium chloride the enzyme dissociates into trimeric units with little or no change in the secondary or tertiary structure and a 15% loss of activity. At higher concentrations the enzyme undergoes sharp unfolding transitions. When the concentration is lowered from 6M to 0.55 M the enzyme refolds in an efficient manner to form trimeric units with more than 75% regain of activity

Streptomyces coelicolor

at 0.5 mM guanidinium chloride the enzyme dissociates into trimeric units with little or no change in the secondary or tertiary structure and a 55% increase of activity. At higher concentrations the enzyme undergoes sharp unfolding transitions. When the concentration is lowered from 6 M to 0.55 M the enzyme refolds in an efficient manner to form trimeric units with less than 35% regain of activity

Mycobacterium tuberculosis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
36	-	-	Mycobacterium tuberculosis
1710	-	-	Streptomyces coelicolor

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Release 2023.1 (January 2023)