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Literature summary for 4.2.1.96 extracted from

  • Rho, H.; Jones, C.N.; Rose, R.B.
    Kinetic stability may determine the interaction dynamics of the bifunctional protein DCoH1, the dimerization cofactor of the transcription factor HNF-1alpha (2010), Biochemistry, 49, 10187-10197.
    View publication on PubMed
Search for more literature for 4.2.1.96

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli as GST-tagged enzyme Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinnat detagged mutant T51S enzyme, 13 mg/ml protein from 0.1 M HEPES-Na, pH 7.5, 2% v/v PEG 400, and 2.0 M ammonium sulfate, X-ray diffraction structure determination and analysis at 1.8 A resolution Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
T51S the point mutation at the enzyme tetramer interface overcomes the dissociation barrier of the homotetramer and increases the interaction with HNF-1alpha. Presence of an ordered water molecule at the tetramer interface, which may destabilize the homotetramer Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography, tag cleavage by thrombin, and p-aminobenzamidine affinity chromatography Rattus norvegicus

Renatured (Commentary)

Renatured (Comment) Organism
DCoH2 unfolding through guanidine is reversible, kinetics, equilibrium unfolding data fit to a two-state model with no apparent intermediate, but folding intermediates are detectable. Proposal of an unfolding pathway in which the tetramer unfolds slowly, but the dimer folds reversibly Rattus norvegicus

Synonyms

Synonyms Comment Organism
PCD
-
 Rattus norvegicus
Pterin-4a-carbinolamine dehydratase
-
 Rattus norvegicus

General Information

General Information Comment Organism
metabolism the PCD activity of the homoteterameric enzyme is involved in the aromatic amino acid metabolism Rattus norvegicus
physiological function the bifunctional protein shows two disparate functions, i.e. dimerization cofactor of HNF-1, DCoH1, and pterin-4a-carbinolamine dehydratase, PCD, that are associated with a change in oligomeric state between dimer and tetramer, overview. The PCD activity of homotetramers aids in aromatic amino acidmetabolism Rattus norvegicus