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Literature summary 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

EC Number Organism UniProt Comment Textmining
4.2.1.10 Mycobacterium tuberculosis
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-
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4.2.1.10 Streptomyces coelicolor
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-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.2.1.10 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
4.2.1.10 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.10 36
-
-
 Mycobacterium tuberculosis
4.2.1.10 1710
-
-
 Streptomyces coelicolor