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Literature summary for 5.1.1.4 extracted from

  • Goytia, M.; Chamond, N.; Cosson, A.; Coatnoan, N.; Hermant, D.; Berneman, A.; Minoprio, P.
    Molecular and structural discrimination of proline racemase and hydroxyproline-2-epimerase from nosocomial and bacterial pathogens (2007), PLoS ONE, 2, e885.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.1.1.4

Cloned(Commentary)

Cloned (Comment) Organism
cloned in Escherichia coli as a 6xHis-tag fusion protein Clostridioides difficile

Inhibitors

Inhibitors Comment Organism Structure
pyrrole-2-carboxylic acid
-
 Clostridioides difficile

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
46.7
-
 (25R)-3beta-hydroxycholest-5-en-27-oate substrate: D-proline, Vmax= 0.000017 M/sec Clostridioides difficile
60.2
-
 (25R)-3beta-hydroxycholest-5-en-27-oate substrate: L-proline, Vmax = 0.000027 M/sec Clostridioides difficile

Organism

Organism UniProt Comment Textmining
Clostridioides difficile A8DEZ8
-
-
Clostridioides difficile VPI10463 A8DEZ8
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-proline CdPRAC from Clostridium difficile racemizes both L- and D-Pro but not OH-L/D-Pro or any other natural amino acid Clostridioides difficile D-proline
-
 r
L-proline CdPRAC from Clostridium difficile racemizes both L- and D-Pro but not OH-L/D-Pro or any other natural amino acid Clostridioides difficile VPI10463 D-proline
-
 r

Synonyms

Synonyms Comment Organism
CdPRAC
-
 Clostridioides difficile
proline racemase
-
 Clostridioides difficile

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Clostridioides difficile

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 using NaOAc Clostridioides difficile