Chromosomal Integration and Expression of Two Bacterial α-Acetolactate Decarboxylase Genes in Brewer's Yeast
نویسندگان
چکیده
منابع مشابه
Structure and mechanism of acetolactate decarboxylase.
Acetolactate decarboxylase catalyzes the conversion of both enantiomers of acetolactate to the (R)-enantiomer of acetoin, via a mechanism that has been shown to involve a prior rearrangement of the non-natural (R)-enantiomer substrate to the natural (S)-enantiomer. In this paper, a series of crystal structures of ALDC complex with designed transition state mimics are reported. These structures,...
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چکیده ندارد.
15 صفحه اولPreliminary crystallographic data for the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from brewers' yeast.
Single crystals of the thiamin diphosphate (the vitamin B1 coenzyme)-dependent enzyme pyruvate decarboxylase (EC 4.1.1.1) from brewers' yeast have been grown using polyethylene glycol as a precipitating agent. Crystals of the homotetrameric version alpha 4 of the holoenzyme are triclinic, space group P1, with cell constants a = 81.0, b = 82.4, c = 116.6 A, alpha = 69.5 beta = 72.6, gamma = 62.4...
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Choline kinase was purified approximately 300-fold, in 5% yield, from an autolysate of dried brewers’ yeast. A molecular weight of 67,000 was estimated using a Stokes radius of 33 A, as determined by Sephadex G-200 chromatography. An s~,,,~ of 4.8 S was obtained by sucrose density gradient centrifugation. Enzyme activity was diminished by sulfhydryl inhibitors and stabilized by the presence of ...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1991
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.57.10.2796-2803.1991