Purification of a membrane-bound sorbitol dehydrogenase from Gluconobacter suboxydans
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منابع مشابه
Crystallization and Properties of NAD-Dependent D-Sorbitol Dehydrogenase from Gluconobacter suboxydans IFO 3257.
NAD-dependent D-sorbitol dehydrogenase (EC 1.1.1.14) was crystallized from the cytosolic fraction of Gluconobacter suboxydans IFO 3257. This is the first example of the enzyme crystallized from acetic acid bacteria. The enzyme catalyzed oxidoreduction between D-sorbitol and D-fructose in the presence of NAD or NADH. The crystalline enzyme showed a single sedimentation peak in analytical ultrace...
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A sorbitol dehydrogenase (GoSLDH) from Gluconobacter oxydans G624 (G. oxydans G624) was expressed in Escherichia coli BL21(DE3)-CodonPlus RIL. The complete 1455-bp codon-optimized gene was amplified, expressed, and thoroughly characterized for the first time. GoSLDH exhibited Km and kcat values of 38.9 mM and 3820 s(-1) toward L-sorbitol, respectively. The enzyme exhibited high preference for N...
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It has previously been shown that cell-free extracts of Acetobacter subozydans possess two pathways for the oxidation of sorbitol (1). In the presence of DPN,l fructose is produced; with TPN, sorbose is formed. The primary purpose of this paper is to describe the separation of these two dehydrogenases from each other. The DPN enzyme free from TPN activity has been concentrated about lBfold, whe...
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The GOX1857 gene, which encodes a putative membrane-bound pyrroloquinoline quinone (PQQ)-dependent dehydrogenase in Gluconobacter oxydans ATCC 621H, was characterized. GOX1857 was disrupted and the oxidizing potential of the resulting mutant strain was compared to that of the wild-type. In contrast to the wild-type, the mutant was unable to grow with myo-inositol as the sole energy source and d...
متن کاملA tightly bound quinone functions in the ubiquinone reaction sites of quinoprotein alcohol dehydrogenase of an acetic acid bacterium, Gluconobacter suboxydans.
Quinoprotein alcohol dehydrogenase (ADH) of acetic acid bacteria is a membrane-bound enzyme that functions as the primary dehydrogenase in the ethanol oxidase respiratory chain. It consists of three subunits and has a pyrroloquinoline quinone (PQQ) in the active site and four heme c moieties as electron transfer mediators. Of these, three heme c sites and a further site have been found to be in...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1995
ISSN: 0378-1097
DOI: 10.1016/0378-1097(94)00470-c