The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase

FEBS Lett. 1993 Nov 29;335(1):57-60. doi: 10.1016/0014-5793(93)80438-z.

Abstract

Previously, the E. coli cysG gene product had been shown to sequentially methylate uro'gen III to produce precorrin-2, hence it was given the trivial name uro'gen III methylase. We now report that in addition to methylase activity, the CysG protein catalyses both the NAD+ dependent oxidation of precorrin-2 to sirohydrochlorin, but also the insertion of iron into this oxidized intermediate, thereby producing siroheme. Thus CysG is a multifunctional protein solely responsible for siroheme synthesis from uro'gen III in E. coli, and accordingly is renamed siroheme synthase.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Escherichia coli / enzymology
  • Escherichia coli / genetics*
  • Genes, Bacterial*
  • Heme / analogs & derivatives
  • Heme / biosynthesis
  • Magnetic Resonance Spectroscopy
  • Methylation
  • Methyltransferases / chemistry
  • Methyltransferases / genetics*
  • Methyltransferases / metabolism
  • Molecular Sequence Data
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / genetics*
  • Multienzyme Complexes / metabolism
  • NAD / metabolism
  • NAD / pharmacology
  • Sequence Homology, Amino Acid
  • Uroporphyrinogens / metabolism

Substances

  • Multienzyme Complexes
  • Uroporphyrinogens
  • NAD
  • Heme
  • siroheme
  • Methyltransferases
  • uroporphyrin-III C-methyltransferase