2.3.2.B14: L,D-transpeptidase
This is an abbreviated version!
For detailed information about L,D-transpeptidase, go to the full flat file.
Word Map on EC 2.3.2.B14
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2.3.2.B14
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tuberculosis
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mycobacterium
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carbapenems
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penicillin-binding
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d,d-transpeptidases
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enterococcus
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faecium
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ldtmt2
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transpeptidases
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imipenem
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ertapenem
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muropeptides
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acylenzyme
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clavulanate
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transpeptidation
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d-ala
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lineage-determining
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doripenem
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d,d-carboxypeptidase
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analysis
- 2.3.2.B14
- tuberculosis
- mycobacterium
- carbapenems
-
penicillin-binding
-
d,d-transpeptidases
- enterococcus
- faecium
- ldtmt2
- transpeptidases
- imipenem
- ertapenem
- muropeptides
-
acylenzyme
- clavulanate
-
transpeptidation
- d-ala
-
lineage-determining
- doripenem
- d,d-carboxypeptidase
- analysis
Reaction
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
CLIBASIA_01175, IprQ, L,D-transpeptidase, L,D-transpeptidase 2, L,D-transpeptidase 5, LdtB, LdtBS, LdtF, Ldtfm, Ldtfm217, Ldtfs, LdtMt1, LdtMt2, LdtP, MAB_1530, MAB_3165c, MT0125, MT0501, MT2594, Rv1433, Rv2518c, transpeptidase, YcbB
ECTree
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General Information
General Information on EC 2.3.2.B14 - L,D-transpeptidase
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physiological function
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examination of 323 mycobacterial Ldts and determination into six clades. Mycobacterium smegmatis LdtF belongs to class 6, having structurally divergent catalytic domains containing a 10-residue insertion near the active site and being preferentially acylated by meropenem
physiological function
in a L,D-transpeptidases YcbB/YcbG mutant, production of the L,D-transpeptidase YcbB in combination with elevated synthesis of the (p)ppGpp alarmone by RelA lead to full bypass of the D,D-transpeptidase activity of penicillin-binding proteins and to broad-spectrum beta-lactam resistance. Production of YcbB is sufficient to switch the role of (p)ppGpp from antibiotic tolerance to high-level beta-lactam resistance. Glycosyltransferase PBP1b is an essential partner of YcbB for peptidoglycan polymerization in the presence of beta-lactams
physiological function
LdtP is a periplasmic esterase involved in modification of the lipid A moiety of the lipopolysaccharide. LdtP is able to complement a strain of Escherichia coli lacking all five of the encoded L,D-transpeptidases, expression results in a slow growth phenotype, restores expression of 5 out of 15 muropeptides and alters lipopolysaccharide structure
physiological function
proposed mechanism, the conserved Cys528 carries out a nucleophilic attack on the penultimate residue, meso-diaminopimelic acid, of a tetrapeptide on the donor peptidoglycan strand, resulting in the release of the terminal D-Ala. This acyl-enzyme intermediate is subsequently deacylated via nucleophilic attack of a side chain amino on the meso-diaminopimelic acid on an adjacent acceptor peptidoglycan strand
physiological function
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LdtP is a periplasmic esterase involved in modification of the lipid A moiety of the lipopolysaccharide. LdtP is able to complement a strain of Escherichia coli lacking all five of the encoded L,D-transpeptidases, expression results in a slow growth phenotype, restores expression of 5 out of 15 muropeptides and alters lipopolysaccharide structure
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