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Literature summary for 5.2.1.8 extracted from

  • Jana, B.; Sau, S.
    The helix located between the two domains of a mip-like peptidyl-prolyl cis-trans isomerase is crucial for its structure, stability, and protein folding ability (2012), Biochemistry, 51, 7930-7939.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type rFKBP22, and of mutants rFKBP22D5, rFKBPP22D30, rFKBP22I3, and rFKBP22I6 in Escherichia coli strains SAU1289, SAU1290, SAU1291, SAU1292, and SAU1293, respectively Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information construction of FKBP22 four helix alpha3 mutant variants by various in vitro probes, rFKBP22D5 and rFKBP22D30 are deletion mutants, while rFKBP22I3 and rFKBP22I6 are insertion mutants. The molecular dimensions, dimerization efficiencies, secondary structures, tertiary structures, stabilities, and protein folding abilities of all mutant proteins differ from those of wild-type rFKBP22, but the rapamycin binding affinities of the mutant proteins are affected very little Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
22960
-
2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation Escherichia coli
23300
-
2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation Escherichia coli
23650
-
2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation Escherichia coli
24140
-
2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation Escherichia coli
48910
-
recombinant mutant rFKBP22D30, gel filtration Escherichia coli
60780
-
recombinant wild-type enzyme, gel filtration Escherichia coli
65710
-
recombinant mutant rFKBP22D5, gel filtration Escherichia coli
71180
-
recombinant mutant rFKBP22I3, gel filtration Escherichia coli
80950
-
recombinant mutant rFKBP22I6, gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type rFKBP22, and mutants rFKBP22D5, rFKBPP22D30, rFKBP22I3, and rFKBP22I6 from Escherichia coli strain BL21(DE3) derivatives SAU1289, SAU1290, SAU1291, SAU1292, and SAU1293, respectively, by nickel affinity chromatography Escherichia coli

Renatured (Commentary)

Renatured (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes, urea-induced unfolding of wild-type and mutant enzymes follows a two-state mechanism and is reversible in nature, mechanism, overview Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information peptidyl-prolyl cis-trans isomerase FKBP22 binds FK506 and rapamycin, that are both immunosuppressive drugs Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
dimer 2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation Escherichia coli
More homology modeling of the three-dimensional enzyme structure, structures of the helix alpha3 mutants, overview Escherichia coli

Synonyms

Synonyms Comment Organism
FKBP22
-
Escherichia coli
mip-like peptidyl-prolyl cis-trans isomerase
-
Escherichia coli
Peptidyl-prolyl cis-trans isomerase
-
Escherichia coli
PPIase
-
Escherichia coli

General Information

General Information Comment Organism
additional information length of helix alpha3 contributes significantly to the preservation of the structure, function, and stability of Escherichia coli FKBP22. Homology modeling of the three-dimensional enzyme structure, overview Escherichia coli