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Microbiology 147 (2001), 249-250
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Microbiology (2001), 147, 249-250.
© 2001 Society for General Microbiology

Microbiology Comment

Heterodimeric dihydroxyacetone kinase from a ptsI mutant of Escherichia coli

R. Beutler1, U. Kämpfer1, J. Schaller1 and B. Erni1

Department of Chemistry and Biochemistry, University of Bern, CH-3012 Bern, , Switzerland1

For correspondence. Tel: +41 31 631 4346. Fax: +41 31 631 4887. e-mail: erni{at}ibc.unibe.ch




This article has been cited by other articles:


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C. Siebold, I. Arnold, L. F. Garcia-Alles, U. Baumann, and B. Erni
Crystal Structure of the Citrobacter freundii Dihydroxyacetone Kinase Reveals an Eight-stranded {alpha}-Helical Barrel ATP-binding Domain
J. Biol. Chem., November 28, 2003; 278(48): 48236 - 48244.
[Abstract] [Full Text] [PDF]

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 Proc. Natl. Acad. Sci. USAHome page
C. Siebold, L. F. Garcia-Alles, B. Erni, and U. Baumann
A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase
PNAS, July 8, 2003; 100(14): 8188 - 8192.
[Abstract] [Full Text] [PDF]

This Article
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Copyright © 2001 Society for General Microbiology.