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Information on EC 2.3.2.B14 - L,D-transpeptidase and Organism(s) Escherichia coli and UniProt Accession P22525

for references in articles please use BRENDA:EC2.3.2.B14
preliminary BRENDA-supplied EC number
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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.B14 L,D-transpeptidase
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This record set is specific for:
Escherichia coli
UNIPROT: P22525 not found.
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Word Map
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Generates 3->3 cross-links in peptidoglycan, catalyzing the cleavage of the mDap(3)-D-Ala4 bond of a tetrapeptide donor stem and the formation of a bond between the carbonyl of mDap3 of the donor stem and the side chain of mDap3 of the acceptor stem.
Synonyms
l,d-transpeptidase, ldtmt1, ldtfs, l,d-transpeptidase 5, mt2594, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
peptidoglycan (3->3)-transpepdidase
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
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incubation of YcbB with a disaccharide-tetrapeptide prepared from the peptidoglycan of Escherichia coli results in the formation of a peptidoglycan dimer containing a diaminopimelate3 -diaminopimelate3 cross-link. Purified YcbB uses as the acyl donor a disaccharide-tetrapeptide ending in D-Ala4, but not a disaccharide-pentapeptide ending in D-Ala4-D-Ala5
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Imipenem
treatment leads to full and irreversible acylation of the protein
meropenem
treatment leads to full and irreversible acylation of the protein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of YcbB consists of a conserved L,D-transpeptidase catalytic domain decorated with a subdomain on the dynamic substrate capping loop, peptidoglycan-binding and large scaffolding domains. The YcbB-meropenem complex map has ordered density defining the active site residues including the thiol ester covalent link of Cys528 and acylated meropenem
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hugonnet, J.E.; Mengin-Lecreulx, D.; Monton, A.; den Blaauwen, T.; Carbonnelle, E.; Veckerle, C.; Brun, Y.V.; van Nieuwenhze, M.; Bouchier, C.; Tu, K.; Rice, L.B.; Arthur, M.
Factors essential for L,D-transpeptidase-mediated peptidoglycan cross-linking and beta-lactam resistance in Escherichia coli
eLife
5
e19469
2016
Escherichia coli (P22525)
Manually annotated by BRENDA team
Caveney, N.A.; Caballero, G.; Voedts, H.; Niciforovic, A.; Worrall, L.J.; Vuckovic, M.; Fonvielle, M.; Hugonnet, J.E.; Arthur, M.; Strynadka, N.C.J.
Structural insight into YcbB-mediated beta-lactam resistance in Escherichia coli
Nat. Commun.
10
1849
2019
Escherichia coli (P22525), Escherichia coli
Manually annotated by BRENDA team