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Alternative NAD+-dependent formate dehydrogenases in the facultative methylotrophMycobacterium vaccae10

Authors
Journal
FEMS Microbiology Letters
0378-1097
Publisher
Oxford University Press
Publication Date
Keywords
  • Formate Dehydrogenase
  • Methylotroph
  • Molybdenum
  • Mycobacterium Vaccae
Disciplines
  • Biology

Abstract

Abstract Mycobacterium vaccae 10 growing in methanol medium synthesizes two inducible alternative NAD +-dependent formate dehydrogenases (FDH). In the presence of molybdenum, the dominating form of the enzyme is FDHI with M r 440 kDa and K m 0.32 mM for sodium formate. FDHI reduced ferricyanide as well as NAD +, and it was reversibly inactivated by formate. NAD + stabilized FDHI against this inactivation. Under conditions of artificial molybdenum deficiency (tungsten in the medium), the second enzyme (FDHII) appeared with M r about 93 kDa and K m 8.3 mM for sodium formate, and no FDHI activity was detected. FDHII did not reduce ferricyanide and was not inactivated by formate. The activity of FDHI was restored in tungsten-grown cells by pulse addition of molybdenum under conditions of blocked protein synthesis, suggesting the pre-existence of inactive apo-FDHI.

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