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

Abstract:

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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Publisher copy:
10.1007/s00018-005-5518-0

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
Journal:
Cellular and molecular life sciences : CMLS More from this journal
Volume:
63
Issue:
7-8
Pages:
890-900
Publication date:
2006-04-01
DOI:
EISSN:
1420-9071
ISSN:
1420-682X
Language:
English
Keywords:
Pubs id:
pubs:95135
UUID:
uuid:a7db8fd3-b177-4b26-a005-236138aff36d
Local pid:
pubs:95135
Source identifiers:
95135
Deposit date:
2013-02-20

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