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Literature summary for 3.4.13.9 extracted from

  • Park, M.S.; Hill, C.M.; Li, Y.; Hardy, R.K.; Khanna, H.; Khang, Y.H.; Raushel, F.M.
    Catalytic properties of the PepQ prolidase from Escherichia coli (2004), Arch. Biochem. Biophys., 429, 224-230.
    View publication on PubMed
Search for more literature for 3.4.13.9

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Met-L-Pro + H2O
-
 Escherichia coli L-Met + L-Pro
-
 ?
additional information enzyme additionally catalyzes the stereoselective hydrolysis of organophosphate triesters and organophosphate diesters such as (S)-methyl phenyl 4-nitrophenyl phosphate with 70fold preferrence for the (S)-enantiomer. Enzyme hydrolyzes 4-nitrophenyl analogs of sarin, soman, and VX Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
PepQ
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
109
-
 L-Met-L-Pro
-
 Escherichia coli