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Literature summary for 2.7.1.71 extracted from

  • Saidemberg, D.M.; Passarelli, A.W.; Rodrigues, A.V.; Basso, L.A.; Santos, D.S.; Palma, M.S.
    Shikimate kinase (EC 2.7.1.71) from Mycobacterium tuberculosis: kinetics and structural dynamics of a potential molecular target for drug development (2011), Curr. Med. Chem., 18, 1299-1310.
    View publication on PubMed
Search for more literature for 2.7.1.71

Application

Application Comment Organism
drug development the enzyme is a target for antimicrobial and anti-paarasite drugs Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis and conformational dynamics, overview Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + shikimate Mycobacterium tuberculosis
-
 ADP + 3-phosphoshikimate
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + shikimate
-
 Mycobacterium tuberculosis ADP + 3-phosphoshikimate
-
 ?

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the fifth step in the shikimate pathway Mycobacterium tuberculosis
physiological function he phosphate binding domain in the apo-enzyme is fairly rigid and largely protected from solvent access, even at relatively high temperatures. The shikimate binding domain is highly flexible, the apo-enzyme tends to exhibit large conformational changes to permit LID closure after the shikimate binding. The nucleotide binding domain is initially conformationally rigid, which seems to favour the initial orientation of ADP/ATP, but becomes highly flexible at temperatures above 30°C, which may permit domain rotation. Part of the LID domain, including the phosphate binding site, is partially rigid, while another part is highly flexible and accessible to the solvent, mide H/D exchange and mass spectrometry Mycobacterium tuberculosis