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6.3.2.13: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2,6-diaminopimelate ligase

This is an abbreviated version!
For detailed information about UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2,6-diaminopimelate ligase, go to the full flat file.

Word Map on EC 6.3.2.13

Reaction

ATP
+
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate
 +
meso-2,6-diaminoheptanedioate
=
ADP
 +
phosphate
 +
UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate

Synonyms

amide ligase, Diaminopimelic-adding enzyme, mDAP ligase, Meso-diaminopimelate-adding enzyme, Mur ligase, MurE, MurE synthetase, MurEEr, peptidoglycan MurE ligase, Synthetase, uridine diphospho-N-acetylmuramoylalanyl-D-glutamyl-meso-2,6-diaminopimelate, UDP-MurNAc-tripeptide synthetase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelate synthetase, UDP-N-acetylmuramyl tripeptide synthetase, UDP-N-acetylmuramyl-tripeptide synthetase, UDPMurNAc-L-alanyl-D-glutamate:mDAP ligase (ADP-forming), Uridine diphosphate N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate ligase, Uridine-diphosphate-N-acetylmuramyl-L-alanyl-D-glutamate:meso-2,6-diaminopimelate synthetase

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.13 UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2,6-diaminopimelate ligase

Engineering

Engineering on EC 6.3.2.13 - UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2,6-diaminopimelate ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D399A
site-directed mutagenesis, inactive mutant
D399N
site-directed mutagenesis, almost inactive mutant
F340A
site-directed mutagenesis, almost inactive mutant
F340Y
site-directed mutagenesis, the mutant shows reduced activity with substrate L-alanine and meso-2,6-diaminoheptanedioate compared to wild-type enzyme
H398A
site-directed mutagenesis, the mutant shows reduced activity with substrate L-alanine and meso-2,6-diaminoheptanedioate compared to wild-type enzyme
H398D
site-directed mutagenesis, the mutant shows highly reduced activity with substrate L-alanine and meso-2,6-diaminoheptanedioate compared to wild-type enzyme
N400A
site-directed mutagenesis, the mutant shows reduced activity with substrate L-alanine and meso-2,6-diaminoheptanedioate compared to wild-type enzyme
N400P
site-directed mutagenesis, the mutant shows slightly reduced activity with substrate meso-2,6-diaminoheptanedioate, but increased activity with substrate L-alanine compared to wild-type enzyme
R401A
site-directed mutagenesis, almost inactive mutant
D392A
-
kcat lower than wild-type, Km (meso-2,6-diaminoheptanedioate) and Km (ATP) higher than wild-type, Km (UDP-MurNAc-L-Ala-D-Glu) lower than wild-type, mutant shows hydrolysis of ATP uncoupled from catalysis. The ATP hydrolysis rate is enhanced by at least partial occupation of the uridine nucleotide dipeptide binding site, mutant shows very high activity with all the amino acids, uridine sugar precursors and nucleotides tested compared to wild type and moreover, reaching up to 100%
DELTA1-24
-
N-terminal deletion mutant, kcat comparable to wild-type, Km values comparable to wild-type, mutant shows similar results to the wild-type with all the nucleotides, UDP-MurNAc peptides and amino acids
E220A
-
kcat lower than wild-type, Km (ATP) and Km (UDP-MurNAc-L-Ala-D-Glu), Km (meso-2,6-diaminoheptanedioate) lower than wild-type, mutant shows hydrolysis of ATP uncoupled from catalysis. The ATP hydrolysis rate is enhanced by atleast partial occupation of the uridine nucleotide dipeptide binding site, mutant shows very high activity with all the amino acids, uridine sugar precursors and nucleotides tested compared to wild type and moreover, reaching up to 100%
K157A
-
kcat lower than wild-type, Km (meso-2,6-diaminoheptanedioate), Km (UDP-MurNAc-L-Ala-D-Glu) and Km (ATP) lower than wild-type, mutant shows hydrolysis of ATP uncoupled from catalysis. The ATP hydrolysis rate is enhanced by at least partial occupation of the uridine nucleotide dipeptide binding site, mutant shows very high activity with all the amino acids, uridine sugar precursors and nucleotides tested compared to wild type and moreover, reaching up to 100%
N449D
-
kcat lower than wild-type, Km (ATP) and Km (meso-2,6-diaminoheptanedioate) higher than wild-type, Km (UDP-MurNAc-L-Ala-D-Glu) lower than wild-type, mutant shows similar results to the wild-type with all the nucleotides, UDP-MurNAc peptides and amino acids, except D-Lys, which shows a slightly higher activity for mutant N449D
R451A
-
kcat lower than wild-type, Km (ATP) comparable to wild-type, Km (meso-2,6-diaminoheptanedioate) higher than wild-type, Km (UDP-MurNAc-L-Ala-D-Glu) lower than wild-type, significant activity in the presence of L-Lys, D-Lys, DL-ornithine and D-Glu for mutant R451A with similar activities as wild type for all the nucleotides and UDP-MurNAc peptides tested
additional information