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Literature summary for 3.5.1.11 extracted from

  • Kumar, R.S.; Prabhune, A.A.; Pundle, A.V.; Karthikeyan, M.; Suresh, C.G.
    A tryptophan residue is identified in the substrate binding of penicillin G acylase from Kluyvera citrophila (2007), Enzyme Microb. Technol., 40, 1389-1397.
No PubMed abstract available
Search for more literature for 3.5.1.11

Inhibitors

Inhibitors Comment Organism Structure
2-hydroxy 5-nitrobenzylbromide
-
 Kluyvera cryocrescens
N-bromosuccinamide 0.1 mM, 70% loss of activity Kluyvera cryocrescens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.016
-
 penicillin G unmodified enzyme Kluyvera cryocrescens
0.051
-
 penicillin G enzyme modified with 2-hydroxy 5-nitrobenzylbromide Kluyvera cryocrescens
0.054
-
 penicillin G enzyme modified with N-bromosuccinamide Kluyvera cryocrescens

Organism

Organism UniProt Comment Textmining
Kluyvera cryocrescens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Kluyvera cryocrescens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzylpenicillin + H2O
-
 Kluyvera cryocrescens phenylacetic acid + 6-aminopenicillanate
-
 ?
penicillin G + H2O a tryptophan residue is important for binding substrate penicillin G Kluyvera cryocrescens 6-aminopenicillanate + phenylacetic acid
-
 ?

Synonyms

Synonyms Comment Organism
KcPGA
-
 Kluyvera cryocrescens
penicillin G acylase
-
 Kluyvera cryocrescens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
63
-
 penicillin G unmodified enzyme, enzyme modified with N-bromosuccinamide or enzyme modified with 2-hydroxy 5-nitrobenzylbromide Kluyvera cryocrescens