6.3.2.10: UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase

This is an abbreviated version!
For detailed information about UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase, go to the full flat file.

Word Map on EC 6.3.2.10

Reaction

ATP
+
UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine
+
D-alanyl-D-alanine
=
ADP
+
phosphate
+
UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine

Synonyms

More, UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine synthetase, Synthetase, uridine diphosphoacetylmuramoylpentapeptide, Uridine diphosphoacetylmuramoylpentapeptide synthetase, UDPacetylmuramoylpentapeptide synthetase, D-Ala-D-Ala-adding enzyme, UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine ligase, MurF, MurF1, ATP-dependent UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase, AbMurF

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.2 Acid—amino-acid ligases (peptide synthases)
                6.3.2.10 UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase

Engineering

Engineering on EC 6.3.2.10 - UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A288T
naturally occuring murF2 allele, expressed as a fusion protein with glutathione S-transferase, is 181fold less catalytically active than the wild-type enzyme at 30°c and even more reduced at 42°C
E158A
site-directed mutagenesis, 4520fold reduced activity compared to the wild-type
E158G
site-directed mutagenesis, over 451fold reduced activity compared to the wild-type
E158D
site-directed mutagenesis, 246fold reduced activity compared to the wild-type
H188A
site-directed mutagenesis, 203fold reduced activity compared to the wild-type
H188G
site-directed mutagenesis, 214fold reduced activity compared to the wild-type
H188N
site-directed mutagenesis, 1860fold reduced activity compared to the wild-type
H188D
site-directed mutagenesis, 2990fold reduced activity compared to the wild-type
K202A
-
site-directed mutagenesis, exchange of highly conserved lysine residue leads to highly reduced activity, activity can be rescued best by addition of propionate or other short-chain carboxylic acids, but only in a small extent by amines