Structural elements of bactopterin from Pseudomonas carboxydoflava carbon monoxide dehydrogenase

Biochim Biophys Acta. 1987 Apr 30;912(3):357-64. doi: 10.1016/0167-4838(87)90040-9.

Abstract

Bactopterin is a novel pterin occurring in bacterial molybdoenzymes as the organic portion of the molybdenum cofactor. Its structure is investigated here. The compound contains a single pterin ring and carries a side chain at carbon atom 6 of the pterin nucleus as indicated by the formation of pterin-6-carboxylic acid upon alkaline permanganate oxidation. Studies with phosphate-cleaving enzymes revealed the presence of two monophosphoric acid monoesters. The affinity of reduced bactopterin for thiol-Sepharose points to the presence of thiol(s) in active bactopterin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehyde Oxidoreductases / analysis*
  • Chemical Phenomena
  • Chemistry
  • Chromatography, Gel
  • Coenzymes*
  • Cytosine Nucleotides*
  • Metalloproteins
  • Molybdenum Cofactors
  • Multienzyme Complexes*
  • Oxidation-Reduction
  • Phosphates / analysis
  • Pseudomonas / enzymology*
  • Pteridines
  • Pterins / analysis*
  • Spectrometry, Fluorescence
  • Sulfhydryl Compounds / analysis

Substances

  • Coenzymes
  • Cytosine Nucleotides
  • Metalloproteins
  • Molybdenum Cofactors
  • Multienzyme Complexes
  • Phosphates
  • Pteridines
  • Pterins
  • Sulfhydryl Compounds
  • molybdopterin cytosine dinucleotide
  • molybdenum cofactor
  • Aldehyde Oxidoreductases
  • carbon monoxide dehydrogenase