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6.3.2.8: UDP-N-acetylmuramate-L-alanine ligase

This is an abbreviated version!
For detailed information about UDP-N-acetylmuramate-L-alanine ligase, go to the full flat file.

Word Map on EC 6.3.2.8

Reaction

ATP
+
UDP-N-acetyl-alpha-D-muramate
+
L-alanine
=
ADP
+
phosphate
+
UDP-N-acetyl-alpha-D-muramoyl-L-alanine

Synonyms

Alanine-adding enzyme, alr5065, L-Ala ligase, L-Alanine adding enzyme, Mur ligase, MurB/CVs, MurC, MurC ligase, MurC synthetase, Synthetase, uridine diphospho-N-acetylmuramoylalanine, UDP-acetylmuramoyl-L-alanine synthetase, UDP-MurNAc:L-Ala ligase, UDP-MurNAc:L-alanine ligase, UDP-N-acetylenolpyruvoylglucosamine reductase/UDP-N-acetylmuramate: L-alanine ligase, UDP-N-acetylmuramate-alanine ligase, UDP-N-acetylmuramate:L-alanine ligase, UDP-N-acetylmuramic acid L-alanine ligase, UDP-N-acetylmuramoyl-L-alanine synthetase, UDP-N-acetylmuramoyl:L-alanine ligase, UDP-N-acetylmuramoylalanine synthetase, UDP-N-acetylmuramyl:L-alanine ligase, UNAM:Ala ligase, Uridine 5´-diphosphate-N-acetylmuramyl-L-alanine synthetase, Uridine diphosphate N-acetylmuramate:L-alanine ligase, Uridine diphospho-N-acetylmuramoylalanine synthetase, Uridine-diphosphate-N-acetylmuramate:L-alanine ligase

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.8 UDP-N-acetylmuramate-L-alanine ligase

Engineering

Engineering on EC 6.3.2.8 - UDP-N-acetylmuramate-L-alanine ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T362A/T365A/T51A
-
site-directed mutagenesis, the mutant shows impaired activity
T362A/T365A/T51A/T120A
-
site-directed mutagenesis, the mutant shows impaired activity
T362A/T365A/T51A/T120A/T167A
-
site-directed mutagenesis, the mutant shows impaired activity
T362A/T365A/T51A/T120A/T167A/T133A
-
site-directed mutagenesis, the mutant shows impaired activity
C230A
-
activity completely lost at 42°C
C426A
-
Km increased 3fold for ATP and 10fold for UDP-MurNAc and L-alanine, with respect to the wild-type
H199A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
K130A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
N293A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
N296A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
R327A
-
mutant enzymes K130A, H199A, N293A, N296A, and R327A lead to important variations of the Km value for one or more substrates
R151W
-
site-directed mutagenesis
Y246C
-
site-directed mutagenesis
R151W
-
site-directed mutagenesis
-
Y246C
-
site-directed mutagenesis
-
TOF-123
-
mutant enzyme TOF-95 is almost indistinguishable from wild type, mutant enzymes TOF-9 and TOF-123 have alanine-adding activity about 60% of the wild type at both 30 C and 43 C
TOF-9
-
mutant enzyme TOF-95 is almost indistinguishable from wild type, mutant enzymes TOF-9 and TOF-123 have alanine-adding activity about 60% of the wild type at both 30 C and 43 C
TOF-95
-
mutant enzyme TOF-95 is almost indistinguishable from wild type, mutant enzymes TOF-9 and TOF-123 have alanine-adding activity about 60% of the wild type at both 30 C and 43 C
additional information