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Literature summary for 3.4.17.8 extracted from

  • Zhang, W.; Shi, Q.; Meroueh, S.O.; Vakulenko, S.B.; Mobashery, S.
    Catalytic mechanism of penicillin-binding protein 5 of Escherichia coli (2007), Biochemistry, 46, 10113-10121.
    View publication on PubMed
Search for more literature for 3.4.17.8

Cloned(Commentary)

Cloned (Comment) Organism
gene pbp5, expression of wild-type and mutant enzymes in strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
C115S site-directed mutagenesis, truncated mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme Escherichia coli
K213C/C115S site-directed mutagenesis, truncated double mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme Escherichia coli
K47C/C115S site-directed mutagenesis, truncated double mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme Escherichia coli
additional information exchange of active site residues Lys47 and Lys213 for gamma-thialysine, pH-dependency, kinetics, and activity compared to the wild-type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of wild-type and mutant enzymes Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli PBP5 performs a DD-carboxypeptidase reaction on the bacterial peptidoglycan, the major constituent of the cell wall ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from strain BL21(DE3) by ion exchange chromatography, gel filtration, and ultrafiltration Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-/-D-alanine catalytic mechanism involving active site residues Lys47 and Lys213, Lys47 exists in the free-base form for catalysis, Lys213 serves as an electrostatic anchor for the substrate Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diacetyl-L-Lys-D-Ala-D-Ala + H2O
-
 Escherichia coli diacetyl-L-Lys-D-Ala + D-Ala
-
 ?
additional information PBP5 performs a DD-carboxypeptidase reaction on the bacterial peptidoglycan, the major constituent of the cell wall Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
PBP5
-
 Escherichia coli
penicillin-binding protein 5
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.5 10.5
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 pH profile, wild-type and mutant enzymes Escherichia coli