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Crystal structure of a bifunctional deaminase and reductase from Bacillus subtilis involved in riboflavin biosynthesis

Academic Article
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Overview

authors

  • Chen, S. C.
  • Chang, Y. C.
  • Lin, C. H.
  • Lin, Chun-Hung
  • Liaw, S. H.

publication date

  • March 2006

journal

  • Journal of Biological Chemistry  Journal

subject areas

  • Amino Acid Sequence
  • Bacillus subtilis
  • Bacterial Proteins
  • Binding Sites
  • Crystallography, X-Ray
  • Escherichia coli
  • Hydrogen-Ion Concentration
  • Ions
  • Models, Chemical
  • Models, Molecular
  • Molecular Sequence Data
  • NADP
  • Nucleotide Deaminases
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Riboflavin
  • Sequence Homology, Amino Acid
  • Stereoisomerism
  • Substrate Specificity
  • Sugar Alcohol Dehydrogenases
  • Tetrahydrofolate Dehydrogenase
  • Zinc
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M510254200

PubMed ID

  • 16308316
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Additional Document Info

start page

  • 7605

end page

  • 7613

volume

  • 281

issue

  • 11

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