Investigation of the metal-binding site of the metalloenzyme NAD+: 2-oxidoreductase (glycerol dehydrogenase) EC 1.1.1.6 from <i>Bacillus stearothermophilus</i>

Spencer, P.S.; Gore, Michael G.; Bown, Kevin; Scawen, Michael D.; Atkinson, Tony

doi:10.1042/bst0151099

Cited by 3 publications

(1 citation statement)

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“…We have also demonstrated that the structure of the metallo-enzyme and metal-depleted enzyme are different 171. The inactive metal-depleted enzyme can be reactivated by the addition of one of a variety of divalent cations [7], although preliminary data showed that the reactivation process is complex [6]. This paper GDH activity was assayed by following the increase in absorbance at 340 nm at 30°C using a Perkin-Elmer lambda 3 spectrophotometer.…”

Section: Assaymentioning

confidence: 99%

Identification of a reversible structural transition in the metal‐depleted glycerol dehydrogenase from Bacillus stearothermophilus

Spencer

Paine

Scawen³

et al. 1990

FEBS Letters

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Evidence is presented to demonstrate that the Znzf -depleted, inactive form of the glycerol dehydrogenase from BaciNus stearothermophifw exists in one of two possible conformations in equilibrium, the position of which is temperature sensitive. The conformation of the metal-depleted enzyme favoured by higher temperatures (20-4O"C) is able to bind Zn2+ and regain catalytic activity, whereas that favoured at lower temperatures (0-10X') is unable to bind metal ions and is thus inactive. This equilibrium is also pH dependent with a pK of 6.6. At pH 6.0, the equilibrium lies in favour of the form of the enzyme able to bind metal ions and exhibit activity.

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Section: Assaymentioning

confidence: 99%