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

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For detailed information about UDP-N-acetylmuramate-L-alanine ligase, go to the full flat file.

Reaction

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

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Results	in table
7	Activating Compound
39030	AA Sequence
2	Application
1	CAS Registry Number
14	Cloned(Commentary)
13	Cofactor
6	Crystallization (Commentary)
24	General Information
4	General Stability
55	IC50 Value
189	Inhibitors
5	kcat/KM [mM/s]
4	Ki Value [mM]
77	KM Value [mM]
8	Localization
37	Metals/Ions
16	Molecular Weight [Da]
28	Natural Substrates/ Products (Substrates)
451	Organism
7	Pathway
55	PDB ID
15	pH Optimum
3	pH Range
1	pH Stability
1	Posttranslational Modification
21	Protein Variants
15	Purification (Commentary)
5	Reaction
2	Reaction Type
61	Reference
1	Source Tissue
5	Specific Activity [micromol/min/mg]
4	Storage Stability
122	Substrates and Products (Substrate)
8	Subunits
58	Synonyms
1	Systematic Name
10	Temperature Optimum [°C]
3	Temperature Stability [°C]
31	Turnover Number [1/s]

Posttranslational Modification

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Posttranslational Modification on EC 6.3.2.8 - UDP-N-acetylmuramate-L-alanine ligase

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POSTTRANSLATIONAL MODIFICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

phosphoprotein

Corynebacterium glutamicum

-

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

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