Nomenclature
EC number
2.7.1.71
Systematic name
ATP:shikimate 3-phosphotransferase
Recommended name
shikimate kinase
Synonyms
AroK
AroL
SKI
SKII
kinase (phosphorylating), shikimate
kinase, shikimate (phosphorylating)
shikimate kinase II
CAS registry number
9031-51-0
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References
Morell, H.; Sprinson, D.B.: Shikimate kinase isoenzymes in Salmonella typhimurium. J. Biol. Chem., 243, 676–682 (1968)
Koshiba, T.: Alicyclic acid metabolism in plants. 12. Partial purification and some properties of shikimate kinase from Phaseolus mungo seedlings. Plant Cell Physiol., 20, 803–809 (1979)
de Feyter, R.: Shikimate kinases from Escherichia coli K12. Methods Enzymol., 142, 355–361 (1987)
Bode, R.; Birnbaum, D.: Aggregation and separability of the shikimate pathway enzymes in yeasts. Z. Allg. Mikrobiol., 21, 417–422 (1981)
Bode, R.; Kunze, G.: Purification and isolation of the arom aggregates of Schizosaccharomyces pombe. Z. Allg. Mikrobiol., 23, 289–296 (1983)
Cerasoli, E.; Kelly, S.M.; Coggins, J.R.; Lapthorn, A.J.; Clarke, D.T.; Price, N.C.: Effects of salts on the function and conformational stability of shikimate kinase. Biochim. Biophys. Acta, 1648, 43–54 (2003)
Kempner, E.S.; Cole, K.W.; Gaertner, F.H.: The functional unit of the arom conjugate in Neurospora. J. Biol. Chem., 257, 8919–8921 (1982)
Bowen, J.R.; Kosuge, T.: In vivo activity, purification, and characterization of shikimate kinase from Sorghum. Plant Physiol., 64, 382–386 (1979)
DeFeyter, R.C.; Pittard, J.: Purification and properties of shikimate kinase II from Escherichia coli K-12. J. Bacteriol., 165, 331–333 (1986)
Schmidt, C.L.; Daneel, H.-J.; Schultz, G.; Buchanan, B.B.: Shikimate kinase from spinach chloroplasts. Purification, characterization and regulatory function in aromatic amino acid biosynthesis. Plant Physiol., 93, 758–766 (1990)
Duncan, K.; Edwards, R.M.; Coggins, J.R.: The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains. Biochem. J., 246, 375–386 (1987)
Lobner-Olesen, A.; Marinus, M.G.: Identification of the gene (aroK) encoding shikimic acid kinase I of Escherichia coli. J. Bacteriol., 174, 525–529 (1992)
Lumsden, J.; Coggins, J.R.: The subunit structure of the arom multienzyme complex of Neurospora crassa. A possible pentafunctional polypeptide chain. Biochem. J., 161, 599–607 (1977)
Romanowski, M.J.; Burley, S.K.: Crystal structure of the Escherichia coli shikimate kinase I (AroK) that confers sensitivity to mecillinam. Proteins Struct. Funct. Genet., 47, 558–562 (2002)
Gu, Y.; Reshetnikova, L.; Li, Y.; Wu, Y.; Yan, H.; Singh, S.; Ji, X.: Crystal structure of shikimate kinase from Mycobacterium tuberculosis reveals the dynamic role of the LID domain in catalysis. J. Mol. Biol., 319, 779–789 (2002)
Krell, T.; Coyle, J.E.; Horsburgh, M.J.; Coggins, J.R.; Lapthorn, A.J.: Crystallization and preliminary X-ray crystallographic analysis of shikimate kinase from Erwinia chrysanthemi. Acta Crystallogr. Sect. D, D53, 612–614 (1997)
Krell, T.; Coggins, J.R.; Lapthorn, A.J.: The three-dimensional structure of shikimate kinase. J. Mol. Biol., 278, 983–997 (1998)
Daugherty, M.; Vonstein, V.; Overbeek, R.; Osterman, A.: Archaeal shikimate kinase, a new member of the GHMP-kinase family. J. Bacteriol., 183, 292–300 (2001)
Cerasoli, E.; Kelly, S.M.; Coggins, J.R.; Boam, D.J.; Clarke, D.T.; Price, N.C.: The refolding of type II shikimate kinase from Erwinia chrysanthemi after denaturation in urea. Eur. J. Biochem., 269, 2124–2132 (2002)
Whipp, M.J.; Pittard, A.J.: A reassessment of the relationship between aroK-and aroL-encoded shikimate kinase enzymes of Escherichia coli. J. Bacteriol., 177, 1627–1629 (1995)
Krell, T.; Maclean, J.; Boam, D.J.; Cooper, A.; Resmini, M.; Brocklehurst, K.; Kelly, S.M.; Price, N.C.; Lapthorn, A.J.; Coggins, J.R.: Biochemical and X-ray crystallographic studies on shikimate kinase: the important structural role of the P-loop lysine. Protein Sci., 10, 1137–1149 (2001)
Oliveira, J.S.; Pinto, C.A.; Basso, L.A.; Santos, D.S.: Cloning and overexpression in soluble form of functional shikimate kinase and 5-enolpyruvylshikimate 3-phosphate synthase enzymes from Mycobacterium tuberculosis. Protein Expr. Purif., 22, 430–435 (2001)
Idziak, C.; Price, N.C.; Kelly, S.M.; Krell, T.; Boam, D.J.; Lapthorn, A.J.; Coggins, J.R.: The interaction of shikimate kinase from Erwinia chrysanthemi with substrates. Biochem. Soc. Trans., 25, S627 (1997)
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(2007). Shikimate kinase. In: Schomburg, D., Schomburg, I., Chang, A. (eds) Class 2 • Transferases IX. Springer Handbook of Enzymes, vol 36. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-47815-7_34
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