Glycerol Dehydratases: Biochemical Structures,Catalytic Mechanisms,and Industrial Applications in 1,3-Propanediol Production by Naturally Occurring and Genetically Engineered Bacterial Strains |
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| Authors: | Jian-zhong?Liu,Wu?Xu,Andrei?Chistoserdov author-information" > author-information__contact u-icon-before" > mailto:ayc@louisiana.edu" title=" ayc@louisiana.edu" itemprop=" email" data-track=" click" data-track-action=" Email author" data-track-label=" " >Email author,Rakesh?K.?Bajpai |
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| Affiliation: | 1.Hubei Coal Conversion and New Carbon Materials Key Laboratory College of Chemical Engineering and Technology,Wuhan University of Science and Technology,Wuhan,China;2.Department of Chemistry,University of Louisiana at Lafayette,Lafayette,USA;3.Department of Biology,University of Louisiana at Lafayette,Lafayette,USA;4.Department of Chemical Engineering,University of Louisiana at Lafayette,Lafayette,USA |
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| Abstract: | To date, two types of glycerol dehydratases have been reported: coenzyme B12-dependent and coenzyme B12-independent glycerol dehydratases. The three-dimensional structure of the former is a dimer of αβγ heterotrimer, while that of the latter is a homodimer. Their mechanisms of reaction are typically enzymatic radical catalysis. Functional radical in both the glycerol dehydratases is the adenosyl radical. However, the adenosyl radical in the former originates from coenzyme B12 by homolytic cleavage, and that in the latter from S-adenosyl-methionine. Until some years ago, Clostridium butyricum VPI 1718 was the only microorganism known to possess B12-independent glycerol dehydratase, but since then, several other bacteria with this unique capability have been identified. This article focuses on the glycerol dehydratases and on 1,3-propanediol production from glycerol by naturally occurring and genetically engineered bacterial strains containing glycerol dehydratase. |
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