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  Biosynthesis of riboflavin in archaea studies on the mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus jannaschii

Fischer, M., Römisch, W., Schiffmann, S., Kelly, M., Oschkinat, H., Steinbacher, S., et al. (2002). Biosynthesis of riboflavin in archaea studies on the mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus jannaschii. Journal of Biological Chemistry, 277(44), 41410-41416.

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Genre: Journal Article
Alternative Title : J. Biol. Chem.

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 Creators:
Fischer, M., Author
Römisch, W., Author
Schiffmann, S., Author
Kelly, M., Author
Oschkinat, H.1, Author              
Steinbacher, S.2, Author              
Huber, R.2, Author              
Eisenreich, W., Author
Richter, G., Author
Bacher, A., Author
Affiliations:
1External Organizations, ou_persistent22              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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 Abstract: The hypothetical protein predicted by the open reading frame MJ0055 of Methanococcus jannaschii was expressed in a recombinant Escherichia coli strain under the control of a synthetic gene optimized for translation in an eubacterial host. The recombinant protein catalyzes the formation of the riboflavin precursor 3,4-dihydroxy-2-butanone 4-phosphate from ribulose 5-phosphate at a rate of 174 nmol mg(-1) min(-1) at 37 degreesC. The homodimeric 51.6-kDa protein requires divalent metal ions, preferentially magnesium, for activity. The reaction involves an intramolecular skeletal rearrangement as shown by C-13 NMR spectroscopy using [U-C-13(5)]ribulose 5- phosphate as substrate. A cluster of charged amino acid residues comprising arginine 25, glutamates 26 and 28, and aspartates 21 and 30 is essential for catalytic activity. Histidine 164 and glutamate 185 were also shown to be essential for catalytic activity.

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Language(s): eng - English
 Dates: 2002-11-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41734
ISI: 000178985300016
 Degree: -

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Title: Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 277 (44) Sequence Number: - Start / End Page: 41410 - 41416 Identifier: ISSN: 0021-9258