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Literature summary extracted from

  • Dementin, S.; Bouhss, A.; Auger, G.; Parquet, C.; Mengin-Lecreulx, D.; Dideberg, O.; van Heijenoort, J.; Blanot, D.
    Evidence of a functional requirement for a carbamoylated lysine residue in MurD, MurE and MurF synthetases as established by chemical rescue experiments (2001), Eur. J. Biochem., 268, 5800-5807.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.2.10 acetate activation of mutant K202A Escherichia coli
6.3.2.10 Butyrate activation of mutant K202A Escherichia coli
6.3.2.10 ethylamine slight activation of mutant K202A Escherichia coli
6.3.2.10 formate slight activation of mutant K202A Escherichia coli
6.3.2.10 propionate strong activation of mutant K202A Escherichia coli
6.3.2.10 Propylamine slight activation of mutant K202A Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.2.10 overexpression of wild-type and MurF mutant K202A as His-tagged enzymes in strain JM83 Escherichia coli
6.3.2.13 expresision of His-tagged MurE in Escherichia coli Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.2.10 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 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.2.10 acetate inhibition of wild-type enzyme Escherichia coli
6.3.2.10 Butylamine inhibition of wild-type and mutant K202A; inhibition of wild-type enzyme Escherichia coli
6.3.2.10 Butyrate slight inhibition of wild-type enzyme Escherichia coli
6.3.2.10 ethylamine inhibition of wild-type enzyme Escherichia coli
6.3.2.10 formate inhibition of wild-type enzyme Escherichia coli
6.3.2.10 methylamine inhibition of wild-type enzyme Escherichia coli
6.3.2.10 propionate inhibition of wild-type enzyme Escherichia coli
6.3.2.10 Propylamine inhibition of wild-type enzyme Escherichia coli
6.3.2.13 Butylamine 500 mM, 88% inhibition Escherichia coli
6.3.2.13 Butyrate 500 mM, 44% inhibition Escherichia coli
6.3.2.13 ethylamine 500 mM, 73% inhibition Escherichia coli
6.3.2.13 methylamine 500 mM, 80% inhibition Escherichia coli
6.3.2.13 Propylamine 500 mM, 87% inhibition Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.3.2.13 cytoplasm
-
 Escherichia coli 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.10 Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.10 ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala Escherichia coli
-
 ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
 ?
6.3.2.13 ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate Escherichia coli
-
 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.2.10 Escherichia coli
-
-
-
6.3.2.13 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.10 recombinant wild-type and mutant enzyme from strain JM83 Escherichia coli
6.3.2.13 recombinant MurE Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.2.10 0.006
-
 purified recombinant mutant K202A, in presence of butylamine Escherichia coli
6.3.2.10 0.016
-
 purified recombinant mutant K202A Escherichia coli
6.3.2.10 0.032
-
 purified recombinant mutant K202A, in presence of propylamine Escherichia coli
6.3.2.10 0.046
-
 purified recombinant mutant K202A, in presence of ethylamine Escherichia coli
6.3.2.10 0.052
-
 purified recombinant mutant K202A, in presence of formate Escherichia coli
6.3.2.10 0.437
-
 purified recombinant mutant K202A, in presence of butyrate Escherichia coli
6.3.2.10 0.511
-
 purified recombinant mutant K202A, in presence of acetate Escherichia coli
6.3.2.10 0.55
-
 purified recombinant wild-type enzyme, in presence of methylamine Escherichia coli
6.3.2.10 0.71
-
 purified recombinant wild-type enzyme, in presence of propylamine Escherichia coli
6.3.2.10 0.72
-
 purified recombinant wild-type enzyme, in presence of butylamine Escherichia coli
6.3.2.10 0.76
-
 purified recombinant wild-type enzyme, in presence of propionate Escherichia coli
6.3.2.10 0.769
-
 purified recombinant mutant K202A, in presence of propionate Escherichia coli
6.3.2.10 0.8
-
 purified recombinant wild-type enzyme, in presence of ethylamine Escherichia coli
6.3.2.10 0.88
-
 purified recombinant wild-type enzyme, in presence of acetate Escherichia coli
6.3.2.10 0.93
-
 purified recombinant wild-type enzyme, in presence of formate Escherichia coli
6.3.2.10 1.24
-
 purified recombinant wild-type enzyme, in presence of butyrate Escherichia coli
6.3.2.10 1.27
-
 purified recombinant wild-type enzyme Escherichia coli
6.3.2.13 0.0047
-
 K224A mutant Escherichia coli
6.3.2.13 0.078
-
 K224A mutant, in the presence of 500 mM propionate Escherichia coli
6.3.2.13 1.24
-
 recombinant wild-type MurE Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.2.10 ATP + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys + D-Ala-D-Ala
-
 Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala
-
 ?
6.3.2.13 ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate
-
 Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.2.10 D-Ala-D-Ala-adding enzyme
-
 Escherichia coli
6.3.2.10 Synthetase, uridine diphosphoacetylmuramoylpentapeptide
-
 Escherichia coli
6.3.2.10 UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine synthetase
-
 Escherichia coli
6.3.2.10 UDP-N-acetylmuramoylalanyl-D-glutamyl-lysine-D-alanyl-D-alanine ligase
-
 Escherichia coli
6.3.2.10 UDPacetylmuramoylpentapeptide synthetase
-
 Escherichia coli
6.3.2.10 Uridine diphosphoacetylmuramoylpentapeptide synthetase
-
 Escherichia coli
6.3.2.13 MurE
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.2.10 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.2.10 8.6
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.10 ATP
-
 Escherichia coli