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Literature summary for 3.4.16.4 extracted from

  • Nicola, G.; Peddi, S.; Stefanova, M.; Nicholas, R.A.; Gutheil, W.G.; Davies, C.
    Crystal structure of Escherichia coli penicillin-binding protein 5 bound to a tripeptide boronic acid inhibitor: A role for Ser-110 in deacylation (2005), Biochemistry, 44, 8207-8217.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure at 1.6 A resolution of PBP5 in complex with a substrate-like peptide boronic acid, suggesting a hydrogen-bonding network, involving Lys-213, Ser-110, and a bridging water molecule, to polarize the hydrolytic water molecule Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Boc-gamma-D-Glu-L-Lys-(Cbz)-D-boroAla-(-)-pinanediol effective inhibitor of the D-alanine CPase activity of PBP5 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.4
-
 Boc-gamma-D-Glu-L-Lys-(Cbz)-D-Ala-D-Ala
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AEB2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Boc-gamma-D-Glu-L-Lys-(Cbz)-D-Ala-D-Ala
-
 Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
D-alanine-carboxypeptidase
-
 Escherichia coli
PBP5
-
 Escherichia coli
penicillin-binding protein 5
-
 Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.013
-
 Boc-gamma-D-Glu-L-Lys-(Cbz)-D-boroAla-(-)-pinanediol
-
 Escherichia coli