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Literature summary for 3.4.11.9 extracted from

  • Graham, S.C.; Guss, J.M.
    Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu (2008), Arch. Biochem. Biophys., 469, 200-208.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
mutants E383A, H361A and H243A in complex with substrate L-Val-L-Pro-L-Leu. Substrate interacts with one of the active site metal ions via its terminal amino group Escherichia coli

Protein Variants

Protein Variants Comment Organism
E383A crystallization data. One of the two metal sites is only partially occupied Escherichia coli
H243A crystallization data. Mutant is capable of binding the substrate L-Val-L-Pro-L-Leu Escherichia coli
H361A crystallization data. Mutant has residual catalytic activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P15034
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Val-L-Pro-L-Leu + H2O
-
Escherichia coli L-Val + L-Pro-L-Leu
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