Literature summary for 6.3.2.8 extracted from

Fiuza, M.; Canova, M.J.; Patin, D.; Letek, M.; Zanella-Cleon, I.; Becchi, M.; Mateos, L.M.; Mengin-Lecreulx, D.; Molle, V.; Gil, J.A.
The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine/threonine protein kinase PknA in Corynebacterium glutamicum (2008), J. Biol. Chem., 283, 36553-36563.

Search for more literature for 6.3.2.8

Cloned(Commentary)

Cloned (Comment)	Organism
gene murC, expression of N-terminally His-tagged wild-type and mutant enzymes as soluble proteins in Escherichia coli strain BL21(DE3), cloning in Corynebacterium glutamicum strain ATCC 13869	Corynebacterium glutamicum

Protein Variants

Protein Variants	Comment	Organism
additional information	mutation of the phosphorylation site threonine residues highly impairs enzyme activity	Corynebacterium glutamicum
T362A/T365A/T51A	site-directed mutagenesis, the mutant shows impaired activity	Corynebacterium glutamicum
T362A/T365A/T51A/T120A	site-directed mutagenesis, the mutant shows impaired activity	Corynebacterium glutamicum
T362A/T365A/T51A/T120A/T167A	site-directed mutagenesis, the mutant shows impaired activity	Corynebacterium glutamicum
T362A/T365A/T51A/T120A/T167A/T133A	site-directed mutagenesis, the mutant shows impaired activity	Corynebacterium glutamicum

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Corynebacterium glutamicum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
52000	-	x * 52000, recombinant detagged enzyme, SDS-PAGE	Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + UDP-N-acetylmuramate + L-alanine	Corynebacterium glutamicum	MurC is essential for peptidoglycan biosynthesis and is responsible of the addition of the first residue L-alanine onto the nucleotide precursor UDP-MurNAc. It is regulated by the serine/threonine protein kinase PknA, overview	ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine	-	?
additional information	Corynebacterium glutamicum	regulation by reversible phosphorylation, overview	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	-	gene murC	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	MurC is phosphorylated in vitro by the PknA protein kinase, but not by PknG kinase, exclusively on threonine residues, which has regulatory function, mutation of the phosphorylation site threonine residues impairs enzyme activity, double phosphorylation of the activation loop residues Thr179 and Thr181 is necessary for full kinase activity	Corynebacterium glutamicum

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3), the His-tag is cleaved off by TEV protease	Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + UDP-N-acetylmuramate + L-alanine	-	Corynebacterium glutamicum	ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine	-	?
ATP + UDP-N-acetylmuramate + L-alanine	MurC is essential for peptidoglycan biosynthesis and is responsible of the addition of the first residue L-alanine onto the nucleotide precursor UDP-MurNAc. It is regulated by the serine/threonine protein kinase PknA, overview	Corynebacterium glutamicum	ADP + phosphate + UDP-N-acetylmuramoyl-L-alanine	-	?
additional information	regulation by reversible phosphorylation, overview	Corynebacterium glutamicum	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 52000, recombinant detagged enzyme, SDS-PAGE	Corynebacterium glutamicum

Synonyms

Synonyms	Comment	Organism
MurC ligase	-	Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.6	-	assay at	Corynebacterium glutamicum

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Corynebacterium glutamicum

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Release 2023.1 (January 2023)