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Literature summary for 3.5.3.3 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

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Substrates and Products (Substrate)

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