Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.8.5.3 extracted from

  • Masui, H.; Fukase, Y.; Satoh, T.
    Accumulation on the cytoplasmic membrane of the precursor to dimethyl sulfoxide reductase in molybdenum cofactor-deficient mutants of Rhodobacter sphaeroides f. sp. denitrificans (1992), Plant Cell Physiol., 33, 463-469.
No PubMed abstract available

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum the molybdenum cofactor is necessary for proteolytic processing of the precursor to the mature enzyme on the periplasmic side of the membrane, whereas binding of the precursor to the membrane and translocation across it can occur in the absence of the cofactor Cereibacter sphaeroides

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the molybdenum cofactor is necessary for proteolytic processing of the precursor to the mature enzyme on the periplasmic side of the membrane, whereas binding of the precursor to the membrane and translocation across it can occur in the absence of the cofactor Cereibacter sphaeroides

General Information

General Information Comment Organism
physiological function more than 50% of chlorate-resistant mutants isolated are defective in the biosynthesis of the molybdenum cofactor and all of these mutants accumulate the precursor form of the enzyme. About 45% of the mutants contain the same level of molybdenum cofactor as the parent strain and exhibit normal levels of DMSO reductase and nitrate reductase activities when chlorate is absent from the medium, but the activities of these enzymes are depressed when chlorate is present. Much of the accumulated precursor form of the enzyme in a molybdenum cofactor-deficient mutant is bound to the cytoplasmic membrane and is sensitive to treatment with proteinase K from the periplasmic side of the membrane. Results suggest that the molybdenum cofactor is necessary for proteolytic processing of the precursor to the mature enzyme on the periplasmic side of the membrane, whereas binding of the precursor to the membrane and translocation across it can occur in the absence of the cofactor Cereibacter sphaeroides