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Literature summary extracted from

  • Siebold, C.; Garcia-Alles, L.F.; Erni, B.; Baumann, U.
    A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase (2003), Proc. Natl. Acad. Sci. USA, 100, 8188-8192.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.29 overexpression in Escherichia coli Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.29 DhaK and DhaK-dihydroxacetone complex are crystallized from 80 mM sodium acetate, pH 5.0, 160 mM ammonium sulfate, 17% polyethylene glycol 4000, 15% 2-methyl-2,4-pentanediol using hanging drop vapor diffusion, crystals diffract to 1.75 A resolution Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.29 Escherichia coli P37349
-
-
2.7.1.29 Escherichia coli P76014
-
-
2.7.1.29 Escherichia coli P76015
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.29 DEAE-cellulose, ResourceQ, Superdex 200 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.29 phospho-DhaM + 3,4-dihydroxy-2-butanone
-
 Escherichia coli dephospho-DhaM + 3-hydroxy-2-butanone-4-phosphate
-
 ?
2.7.1.29 phospho-DhaM + erythrose
-
 Escherichia coli dephospho-DhaM + erythrose 4-phosphate
-
 ?
2.7.1.29 phospho-DhaM + glyceraldehyde
-
 Escherichia coli dephospho-DhaM + glyceraldehyde 2-phosphate
-
 ?