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Literature summary for 3.4.16.4 extracted from

  • Chowdhury, C.; Nayak, T.R.; Young, K.D.; Ghosh, A.S.
    A weak DD-carboxypeptidase activity explains the inability of PBP 6 to substitute for PBP 5 in maintaining normal cell shape in Escherichia coli (2010), FEMS Microbiol. Lett., 303, 76-83.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.16.4

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 Star cells Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.28
-
 Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala recombinant PBP 6, in 50 mM Tris-HCl, pH 8.5, at 37°C Escherichia coli
1.38
-
 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C Escherichia coli
8.98
-
 Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
 purified recombinant PBP 6 Escherichia coli
40000
-
 purified recombinant PBP 5 Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli enzyme removes the terminal D-alanine from the pentapeptide side chains of muramic acid in peptidoglycan ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ampicillin-coupled activated CH-Sepharose 4B resin column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O only substrate of penicillin-binding protein 5, but not of penicillin-binding protein 6 Escherichia coli ?
-
 ?
additional information enzyme removes the terminal D-alanine from the pentapeptide side chains of muramic acid in peptidoglycan Escherichia coli ?
-
 ?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O
-
 Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
DD-Carboxypeptidase
-
 Escherichia coli
DD-CPase
-
 Escherichia coli
PBP 5 the DD-carboxypeptidase activity of PBP 5 is higher than that of PBP 6 Escherichia coli
PBP 6 the DD-carboxypeptidase activity of PBP 6 is lower than that of PBP 5 Escherichia coli
penicillin-binding protein
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.56
-
 Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala recombinant PBP 6, in 50 mM Tris-HCl, pH 8.5, at 37°C Escherichia coli
1.41
-
 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C Escherichia coli
2.7
-
 Nalpha,Nepsilon-Diacetyl-L-Lys-D-Ala-D-Ala recombinant PBP 5, in 50 mM Tris-HCl, pH 8.5, at 37°C Escherichia coli

General Information

General Information Comment Organism
physiological function the DD-carboxypeptidase activity of PBP 5 is responsible for maintaining cell shape Escherichia coli