Literature summary for 3.4.16.4 extracted from

Nicholas, R.A.; Krings, S.; Tomberg, J.; Nicola, G.; Davies, C.
Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex (2003), J. Biol. Chem., 278, 52826-52833.

Search for more literature for 3.4.16.4

Crystallization (Commentary)

Crystallization (Comment)	Organism
vapor diffusion hanging drop technique. Three-dimensional structure of a soluble form of wild-type enzyme at 1.85 A resolution and structure of the G105D mutant form at 1.9 A resolution	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
DELTA74-90	deletion of the 74-90 loop markedly diminishes the deacylation rate of penicillin G with a minimal impact on acylation, and abolishes D-alanine carboxypeptidase activity	Escherichia coli
G105D	mutation markedly impairs deacylation with only minor effects on acylation, and abolishes D-alanine carboxypeptidase activity	Escherichia coli
S86A	mutation has little effect on the interaction of the protein with penicillin G, acylation rate constants are nearly identical to wild-type enzyme. The ratio of turnover number to Km-value for the substrate N,N-diacetyl-L-Lys-D-Ala-D-Ala is 12% of the wild-type ratio	Escherichia coli
S86A/S87A	mutation has little effect on the interaction of the protein with penicillin G, acylation rate constants are nearly identical to wild-type enzyme. The ratio of turnover number to Km-value for the substrate N,N-diacetyl-L-Lys-D-Ala-D-Ala is 8.1% of the wild-type ratio	Escherichia coli
S87A	mutation has little effect on the interaction of the protein with penicillin G, acylation rate constants are nearly identical to wild-type enzyme. The ratio of turnover number to Km-value for the substrate N,N-diacetyl-L-Lys-D-Ala-D-Ala is 6.3% of the wild-type ratio	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	the ratio of turnover number to Km-value for the substrate Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala is 32/Ms for the wild-type enzyme, 3.9/Ms for the S86A mutant, 2.0/Ms for the S87A mutant and 2.6/Ms for the S86A/S87A mutant enzyme	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

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.
additional information	forms a covalent acyl-enzyme complex with beta-lactam antibiotics, high rate of decylation of the acyl-enzyme complex. Direct role for the SXN motif in deacylation of the acyl-enzyme complex. Functioning of this motif is modulated by the 74-90 loop. Ser86 and Ser87 are important for D-alanine carboxypeptidase activity	Escherichia coli	?	-	?
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O	-	Escherichia coli	N,N'-diacetyl-L-Lys-D-Ala + D-Ala	-	?

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	the ratio of turnover number to Km-value for the substrate Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala is 32/Ms for the wild-type enzyme, 3.9/Ms for the S86A mutant, 2.0/Ms for the S87A mutant and 2.6/Ms for the S86A/S87A mutant enzyme	Escherichia coli

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Release 2023.1 (January 2023)