Literature summary for 6.3.2.10 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.

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Activating Compound

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

Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of wild-type and MurF mutant K202A as His-tagged enzymes in strain JM83	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
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

Inhibitors	Comment	Organism	Structure
acetate	inhibition of wild-type enzyme	Escherichia coli
Butylamine	inhibition of wild-type and mutant K202A; inhibition of wild-type enzyme	Escherichia coli
Butyrate	slight inhibition of wild-type enzyme	Escherichia coli
ethylamine	inhibition of wild-type enzyme	Escherichia coli
formate	inhibition of wild-type enzyme	Escherichia coli
methylamine	inhibition of wild-type enzyme	Escherichia coli
propionate	inhibition of wild-type enzyme	Escherichia coli
Propylamine	inhibition of wild-type enzyme	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzyme from strain JM83	Escherichia coli

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli

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Release 2023.1 (January 2023)