Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

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

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.B14 L,D-transpeptidase

Engineering

Engineering on EC 2.3.2.B14 - L,D-transpeptidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C354A
C354S
-
no acylation by beta-lactams is observed
H336A
no cysteine acylation by inhibitors can be detected in a 0-500-s time frame
H352A
mutation does not show a decrease in the rate of the acylation reaction by inhibitors
C354A
-
mutant does not display adduct formation with inhibitors faropenem or 6-aminopenicillanic acid
-
H336A
-
no cysteine acylation by inhibitors can be detected in a 0-500-s time frame
-
H352A
-
mutation does not show a decrease in the rate of the acylation reaction by inhibitors
-
D353A
-
meropenem preferentially acylates the mutant in a competition experiment
D353N
-
meropenem preferentially acylates the mutant in a competition experiment
D353W
-
meropenem preferentially acylates the mutant in a competition experiment. Substitution nearly abolishes acylation by biapenem but does not affect acylation by faropenem, doripenem, or meropenem