2006
DOI: 10.1099/mic.0.28848-0
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Cloning and expression of the gene for periplasmic poly(vinyl alcohol) dehydrogenase from Sphingomonas sp. strain 113P3, a novel-type quinohaemoprotein alcohol dehydrogenase

Abstract: A gene for periplasmic poly(vinyl alcohol) (PVA) dehydrogenase (PVADH) was cloned, based on the N-terminal amino acid sequence of the purified PVADH from Sphingomonas sp. 113P3 and the sequence of the gene for PVADH (pvaA, GenBank accession no. AB190288). The recombinant PVADH tagged with hexahistidine was expressed in Escherichia coli and purified to homogeneity. The recombinant enzyme had the same characteristics as the purified enzyme from Sphingomonas sp. strain 113P. In addition to PVA, the recombinant PV… Show more

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Cited by 33 publications
(15 citation statements)
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“…Cytochrome c has been suggested to be a natural electron acceptor for PVA-DH in vivo. 49) PVA-DH is a member of the type-II quinohemoprotein alcohol dehydrogenases, 50) but the position of the amino acid sequences for the hemebinding domain and superbarrel domain found in this family are the reverse of those of the other members. This is considered significant in terms of the ability of PVA-DH to react with a macromolecule such as PVA.…”
Section: Microbial Degradation Of Synthetic Water-soluble Polymersmentioning
confidence: 98%
“…Cytochrome c has been suggested to be a natural electron acceptor for PVA-DH in vivo. 49) PVA-DH is a member of the type-II quinohemoprotein alcohol dehydrogenases, 50) but the position of the amino acid sequences for the hemebinding domain and superbarrel domain found in this family are the reverse of those of the other members. This is considered significant in terms of the ability of PVA-DH to react with a macromolecule such as PVA.…”
Section: Microbial Degradation Of Synthetic Water-soluble Polymersmentioning
confidence: 98%
“…The PVADH is also designated with the systematic name polyvinyl alcohol: ferricytochrome-c oxidoreductase, which reflects the observation that the enzymatic oxidation of PVA is coupled to the respiratory chain of the microbe via the heme-containing redoxprotein cytochrome c. Such a coupling could not be observed with PVA oxidases. Although PVADH could be successfully cloned and heterologously expressed [75], a non-quino-hemoprotein PVA oxidase has not yet been cloned [76].…”
Section: Enzymesmentioning
confidence: 98%
“…VM15C [22,23] and Sphingopyxis sp. 113P3 [7,12,13] have been registered in GenBank. PVA-DH and OPH from these two strains have similar enzymatic properties and their amino acid sequences show high similarities, 54 and 63%, respectively.…”
Section: Introductionmentioning
confidence: 99%