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Literature summary for 2.7.1.29 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)

Cloned (Comment) Organism
overexpression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Escherichia coli P37349
-
-
Escherichia coli P76014
-
-
Escherichia coli P76015
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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