Small substrate, big surprise: fold, function and phylogeny of dihydroxyacetone kinases.

Journal article

Dihydroxyacetone (Dha) kinases are a family of sequence-conserved enzymes which utilize either ATP (in animals, plants and eubacteria) or phosphoenolpyruvate (PEP, in eubacteria) as their source of high-energy phosphate. The kinases consist of two domains/subunits: DhaK, which binds Dha covalently in hemiaminal linkage to the Nepsilon2 of a histidine, and DhaL, an eight-helix barrel that contains the nucleotide-binding site. The PEP-dependent kinases comprise a third subunit, DhaM, which reph...

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Authors: Erni, B; Siebold, C; Christen, S; Srinivas, A; Oberholzer, A

• Journal: Cellular and molecular life sciences : CMLS
• Volume: 63
• Issue: 7-8
• Pages: 890-900
• Publication date: 2006-04-01
• DOI: 10.1007/s00018-005-5518-0
• EISSN: 1420-9071
• ISSN: 1420-682X
• Language: English
• Keywords: Protein Binding; Dihydroxyacetone; Protein Folding; Phosphotransferases (Alcohol Group Acceptor); Phylogeny; Citrobacter freundii; Models, Molecular