Crystallography of Metabolic Enzymes

Methods Mol Biol. 2020:2096:125-139. doi: 10.1007/978-1-0716-0195-2_10.

Abstract

The metabolic enzymes like any enzymes generally display globular architecture where secondary structure elements and interactions between them preserve the spatial organization of the protein. A typical enzyme features a well-defined active site, designed for selective binding of the reaction substrate and facilitating a chemical reaction converting the substrate into a product. While many chemical reactions could be facilitated using only the functional groups that are found in proteins, the large percentage or intracellular reactions require use of cofactors, varying from single metal ions to relatively large molecules like numerous coenzymes, nucleotides and their derivatives, dinucleotides or hemes. Quite often these large cofactors become important not only for the catalytic function of the enzyme but also for the structural stability of it, as those are buried deep in the enzyme.

Keywords: Cofactors; Metabolic channels; Metabolic enzymes; X-ray diffraction.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Alcohol Oxidoreductases / chemistry
  • Binding Sites
  • Coenzymes / metabolism
  • Crystallization
  • Crystallography, X-Ray / methods*
  • Enzymes / chemistry*
  • Klebsiella pneumoniae / enzymology
  • Models, Molecular
  • NAD / metabolism
  • Stereoisomerism
  • Substrate Specificity

Substances

  • Coenzymes
  • Enzymes
  • NAD
  • Alcohol Oxidoreductases
  • butanediol dehydrogenase