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Literature summary for 5.2.1.8 extracted from

  • Helbig, S.; Patzer, S.I.; Schiene-Fischer, C.; Zeth, K.; Braun, V.
    Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone (2011), J. Biol. Chem., 286, 6280-6290.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
G148D the FkpA313 mutant protein, which contains a G148D replacement in the PPIase domain, shows only a very low in vitro PPIase activity with both peptides (the activity amounts to 0.4 and 0.2% that of wild type enzyme) Escherichia coli
additional information the temperature-sensitive mutant FkpA43 confers 10% activity to colicin M at 30°C and no activity at 42°C, displays a 2fold lower PPIase activity than wild type FkpA for Phe-Pro-176-Val and a 5fold lower activity for Leu-Pro-260-Gly than for Phe-Pro-176-Val (measured at 10°C) Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
FK506
-
Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Escherichia coli
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
colicin M Escherichia coli
-
?
-
?
colicin M Escherichia coli AB2847
-
?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli AB2847
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA-agarose column chromatography and Superdex 75 gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
Escherichia coli 4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
Escherichia coli AB2847 4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
Escherichia coli 4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
Escherichia coli AB2847 4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
?
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
Escherichia coli 4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
?
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
Escherichia coli AB2847 4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
?
colicin M
-
Escherichia coli ?
-
?
colicin M
-
Escherichia coli AB2847 ?
-
?

Synonyms

Synonyms Comment Organism
FkpA
-
Escherichia coli
PPIase
-
Escherichia coli
prolyl cis-trans isomerase
-
Escherichia coli

General Information

General Information Comment Organism
physiological function colicin M unfolds during transfer across the outer or cytoplasmic membrane and refolds to the active form in the periplasm assisted by prolyl cis-trans isomerase/chaperone FkpA Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.45
-
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2 mutant enzyme G148D, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C Escherichia coli
5.11
-
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2 mutant enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C Escherichia coli
96.9
-
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2 wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C Escherichia coli
115
-
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2 wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C Escherichia coli
1380
-
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2 wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C Escherichia coli