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Literature summary for 2.7.1.71 extracted from

  • Dhaliwal, B.; Nichols, C.E.; Ren, J.; Lockyer, M.; Charles, I.; Hawkins, A.R.; Stammers, D.K.
    Crystallographic studies of shikimate binding and induced conformational changes in Mycobacterium tuberculosis shikimate kinase (2004), FEBS Lett., 574, 49-54.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray crystal structure of shikimate kinase with bound shikimate and adenosine diphosphate determined to a resolution of 2.15 A, sitting drop vapor diffusion method Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + shikimate the substrate binds in a pocket lined with hydrophobic residues and interacts with several highly conserved charged residues including Asp34, Arg58,Glu61 and Arg136 which project into the cavity Mycobacterium tuberculosis ADP + shikimate 3-phosphate
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