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Literature summary for 6.3.2.9 extracted from

  • Thakur, M.; Chakraborti, P.K.
    Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis (2008), Biochem. J., 415, 27-33.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene murD, murD is located in a cluster near the other cell division genes such as ftsW, co-expression of GST-tagged MurD with MBP-fusion PknA, a mycobacterial eukaryotic-type serine/threonine kinase, in Escherichia coli BL21(DE3) cells leading to phosphorylation of mMurD. Also overexpression of murD in Mycobacterium smegmatis as His-tagged protein yields a phosphorylated enzyme Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Mycobacterium tuberculosis 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate Mycobacterium tuberculosis the ligase MurD is involved in the process of peptidoglycan biosynthesis by catalyzing the addition of D-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate Mycobacterium tuberculosis H37Ra / ATCC 25177 the ligase MurD is involved in the process of peptidoglycan biosynthesis by catalyzing the addition of D-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis A5U4I2 gene m-murD or Rv2155c
-
Mycobacterium tuberculosis H37Ra / ATCC 25177 A5U4I2 gene m-murD or Rv2155c
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the mycobacterial eukaryotic-type serine/threonine kinase PknA transphosphorylates MurD Mycobacterium tuberculosis

Purification (Commentary)

Purification (Comment) Organism
recombinant recombinant GST-tagged MurD from Escherichia coli by glutathione affinity chromatography, His-tagged MurD from Mycobacterium smegmatis by nickel affinity chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
-
Mycobacterium tuberculosis ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate the ligase MurD is involved in the process of peptidoglycan biosynthesis by catalyzing the addition of D-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine Mycobacterium tuberculosis ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
-
Mycobacterium tuberculosis H37Ra / ATCC 25177 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate the ligase MurD is involved in the process of peptidoglycan biosynthesis by catalyzing the addition of D-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine Mycobacterium tuberculosis H37Ra / ATCC 25177 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
?

Synonyms

Synonyms Comment Organism
MurD
-
Mycobacterium tuberculosis
UDP-N-acetylmuramoyl-L-alanine:D-glutamateligase
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
ATP
-
Mycobacterium tuberculosis