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Literature summary for 3.4.16.4 extracted from

  • Stefanova, M.E.; Davies, C.; Nicholas, R.A.; Gutheil, W.G.
    pH, inhibitor, and substrate specificity studies on Escherichia coli penicillin-binding protein 5 (2002), Biochim. Biophys. Acta, 1597, 292-300.
    View publication on PubMed

General Stability

General Stability Organism
without stabilization dilution of the enzyme to 10 nM results in a 97% loss of activity, whereas with stabilization by bovine serum albumin less than 10% loss of activity is observed Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
diisopropyl fluorophosphate 1 mM, 28% inhibition Escherichia coli
formaldehyde 1 mM, 53% inhibition Escherichia coli
iodoacetamide 1 mM, 20% inhibition Escherichia coli
N-Chlorosuccinimide 1 mM, 50% inhibition Escherichia coli
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala-D-Ala substrate inhibition above 30 mM Escherichia coli
NEM 1 mM, complete inhibition Escherichia coli
p-hydroxymercuribenzoate 1 mM, complete inhibition Escherichia coli
phenylboronic acid 1 mM, 26% inhibition Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Nalpha,Nepsilon-diacetyl-Lys-D-Ala-D-Ala + H2O
-
Escherichia coli Nalpha,Nepsilon-diacetyl-Lys-D-Ala + D-Ala
-
?
Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala-D-Ala + H2O
-
Escherichia coli Nalpha-tert-butoxycarbonyl-Nepsilon-benzyloxycarbonyl-L-Lys-D-Ala + D-Ala
-
?

Synonyms

Synonyms Comment Organism
PBP 5
-
Escherichia coli
penicillin-binding protein 5
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 10
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
8 11 pH 8: about 50% of maximal activity, pH 11: about 50% of maximal activity Escherichia coli