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Literature summary 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)

EC Number Cloned (Comment) Organism
2.7.11.1 expressed in Escherichia coli Mycobacterium tuberculosis
6.3.2.9 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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.1 additional information results of a solid-phase binding assays reveal a high affinity in vitro binding between PknA and mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase mMurD Mycobacterium tuberculosis

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.2.9 Mg2+
-
 Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.2.9 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
-
 ?
6.3.2.9 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

EC Number Organism UniProt Comment Textmining
2.7.11.1 Mycobacterium tuberculosis P9WI83
-
-
2.7.11.1 Mycobacterium tuberculosis H37Rv P9WI83
-
-
6.3.2.9 Mycobacterium tuberculosis A5U4I2 gene m-murD or Rv2155c
-
6.3.2.9 Mycobacterium tuberculosis H37Ra / ATCC 25177 A5U4I2 gene m-murD or Rv2155c
-

Posttranslational Modification

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

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.2.9 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.1 ATP + UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase evidence is provided that mycobacterial mMurD is a substrate of PknA Mycobacterium tuberculosis ADP + phosphorylated-UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase
-
 ?
2.7.11.1 ATP + UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase evidence is provided that mycobacterial mMurD is a substrate of PknA Mycobacterium tuberculosis H37Rv ADP + phosphorylated-UDP-N-acetylmuramoyl-L-alanine:D-glutamate ligase
-
 ?
6.3.2.9 ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
-
 Mycobacterium tuberculosis ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
 ?
6.3.2.9 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
-
 ?
6.3.2.9 ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
-
 Mycobacterium tuberculosis H37Ra / ATCC 25177 ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
 ?
6.3.2.9 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

EC Number Synonyms Comment Organism
2.7.11.1 PknA
-
 Mycobacterium tuberculosis
2.7.11.1 serine-threonine kinase
-
 Mycobacterium tuberculosis
6.3.2.9 MurD
-
 Mycobacterium tuberculosis
6.3.2.9 UDP-N-acetylmuramoyl-L-alanine:D-glutamateligase
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.1 25
-
 assay at Mycobacterium tuberculosis
6.3.2.9 25
-
 assay at Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.1 7.5
-
 assay at Mycobacterium tuberculosis
6.3.2.9 7.5
-
 assay at Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.2.9 ATP
-
 Mycobacterium tuberculosis