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Literature summary extracted from

  • Bazan, J.F.; Weaver, L.H.; Roderick, S.L.; Huber, R.; Matthews, B.W.
    Sequence and structure comparison suggests that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold (1994), Proc. Natl. Acad. Sci. USA, 91, 2473-2477.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.3.3 additional information not a metal-dependent enzyme Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.18 additional information
-
 sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold Escherichia coli
3.5.3.3 additional information
-
 amino acid sequence comparison suggests that the structure of E. coli methionine aminopeptidase and the C-terminal domain of Pseudomonas putida creatinase are related Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.18 Escherichia coli
-
-
-
3.5.3.3 Pseudomonas putida
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.11.18 additional information
-
 a simple assay based upon HPLC Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.3 creatine + H2O
-
 Pseudomonas putida sarcosine + urea
-
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