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Literature summary for 2.7.11.1 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
Search for more literature for 2.7.11.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
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

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WI83
-
-
Mycobacterium tuberculosis H37Rv P9WI83
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PknA
-
 Mycobacterium tuberculosis
serine-threonine kinase
-
 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