NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase

This publication has 25 references indexed in Scilit:

• Cephalopod alcohol dehydrogenase: purification and enzymatic characterization
  FEBS Letters, 1993
• Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase
  Biochemistry, 1992
• Human class III alcohol dehydrogenase/glutathione-dependent formaldehyde dehydrogenase
  Protein Journal, 1991
• Evidence for the identity of glutathione‐dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase
  FEBS Letters, 1989
• 3-Hexulose phosphate synthase from a new facultative methylotroph, Mycobacterium gastri MB19.
  Agricultural and Biological Chemistry, 1988
• The formaldehyde dehydrogenase of Rhodococcus erythropolis, a trimeric enzyme requiring a cofactor and active with alcohols
  European Journal of Biochemistry, 1985
• An unusual formaldehyde oxidizing system inRhodococcus erythropolisgrown on compounds containing methyl groups
  FEMS Microbiology Letters, 1984
• NAD‐dependent, PQQ‐containing methanol dehydrogenase: a bacterial dehydrogenase in a multienzyme complex
  FEBS Letters, 1984
• New human liver alcohol dehydrogenase forms with unique kinetic characteristics
  Biochemical and Biophysical Research Communications, 1981
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976