Purification and characterization of the glucoside 3-dehydrogenase produced by a newly isolated Stenotrophomonas maltrophilia CCTCC M 204024

Zhang, Jianfen; Zheng, Yu‐Guo; Xue, Ya‐Ping; Shen, Yin‐Chu

doi:10.1007/s00253-005-0201-9

Cited by 19 publications

(12 citation statements)

References 20 publications

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“…The inability of trehaloseinduced At7023 cells to convert any of the disaccharides to their respective keto derivatives and their ability to do so when induced with sucrose (Table 2) are consistent with the presence of two distinct enzymes with overlapping activities but stringent requirements for their induction. Therefore, we contend that the 3-ketodisaccharide-forming enzyme encoded by thuAB is functionally similar to but separate from the D-glucoside 3-hydrogenase purified to homogeneity from crude cell extracts of A. tumefaciens by Hayano and Fukui (34) and Vanbeeumen and Deley (43) The presence of 3-ketodisaccharide-forming enzymes has been reported in Flavobacterium sacchrophilum (52), Stenotrophomonas maltrophilia (42), and Halomonas (Deleya) sp. ␣-15 (53).…”

Section: Discussionmentioning

confidence: 93%

The thuEFGKAB Operon of Rhizobia and Agrobacterium tumefaciens Codes for Transport of Trehalose, Maltitol, and Isomers of Sucrose and Their Assimilation through the Formation of Their 3-Keto Derivatives

Ampomah¹,

Avetisyan²,

Hansen³

et al. 2013

Journal of Bacteriology

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eThe thu operon (thuEFGKAB) in Sinorhizobium meliloti codes for transport and utilization functions of the disaccharide trehalose. Sequenced genomes of members of the Rhizobiaceae reveal that some rhizobia and Agrobacterium possess the entire thu operon in similar organizations and that Mesorhizobium loti MAFF303099 lacks the transport (thuEFGK) genes. In this study, we show that this operon is dedicated to the transport and assimilation of maltitol and isomers of sucrose (leucrose, palatinose, and trehalulose) in addition to trehalulose, not only in S. meliloti but also in Agrobacterium tumefaciens. By using genetic complementation, we show that the thuAB genes of S. meliloti, M. loti, and A. tumefaciens are functionally equivalent. Further, we provide both genetic and biochemical evidence to show that these bacteria assimilate these disaccharides by converting them to their respective 3-keto derivatives and that the thuAB genes code for this ketodisaccharide-forming enzyme(s). Formation of 3-ketotrehalose in real time in live S. meliloti is shown through Raman spectroscopy. The presence of an additional ketodisaccharide-forming pathway(s) in A. tumefaciens is also indicated. To our knowledge, this is the first report to identify the genes that code for the conversion of disaccharides to their 3-ketodisaccharide derivatives in any organism. Rhizobia are facultative symbionts which form nitrogen-fixing nodules on leguminous plants (1). Trehalose (␣-D-glucopyranosyl-␣-D-glucopyranoside), which serves as an osmoprotectant in many organisms (2, 3), is found in these symbiotic structures as well as in other structures formed due to interactions between plants and microorganisms (4, 5). In addition to being an osmoprotectant, trehalose is an important source of carbon for microorganisms in agricultural soils. It can originate from nodules during nodule senescence (6) or as an excretion product (7) from mycorrhizal fungi, in which trehalose is an essential storage compound in vegetative cells and spores (8), or from insects and other soil fauna. There are three well-documented pathways for trehalose catabolism in microorganisms: (i) trehalose is hydrolyzed into two glucose moieties by the enzyme trehalase found in Escherichia coli, Bacillus subtilis, and many other microorganisms, including fungi (9); (ii) trehalose is transported across the membranes either by a permease or by a phosphotransferase system (PTS), leaving trehalose unmodified or phosphorylated as trehalose 6-phosphate (T6P) inside the cell (10), and the imported trehalose or T6P is hydrolyzed by enzymes such as trehalase, T6P-hydrolase, phospho-(1-1)-glucosidase or phosphotrehalase (11, 12) to yield both glucose and phosphorylated glucose as products (trehalose phosphorylase may also split trehalose by exerting a phosphate attack on the bond joining the glucose moieties [11; reference 13 and references therein]); and (iii) trehalose is taken up via the PTS as T6P as described above, but in this pathway, the enzyme trehalose-6-phosphate phosphorylase pho...

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Section: Discussionmentioning

confidence: 93%

The thuEFGKAB Operon of Rhizobia and Agrobacterium tumefaciens Codes for Transport of Trehalose, Maltitol, and Isomers of Sucrose and Their Assimilation through the Formation of Their 3-Keto Derivatives

Ampomah¹,

Avetisyan²,

Hansen³

et al. 2013

Journal of Bacteriology

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“…Limoneus [14]; (c) N-bromosuccinimide cleavage of validoxylamine [15,16]; (d) microbial degradation of validamycin A [2,[17][18][19][20][21][22] or acarbose [23]. Among these methods, the degradation of validamycins to produce valienamine with microorganism is one of the most potent methods.…”

Section: Introductionmentioning

confidence: 98%

Enhanced production of valienamine by Stenotrophomonas maltrophilia with fed-batch culture in a stirred tank bioreactor

Xue

Zheng

Shen

2007

Process Biochemistry

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“…The genetic information and characterization of β-glucosidase [9] and glucoside-3-dehydrogenase [10] has been reported. In the case of C-N lyase, it was first identified in F. saccharophilum [7] and purified from cellfree extract [11].…”

Section: Introductionmentioning

confidence: 99%

Gene cloning and expression of a 3-ketovalidoxylamine C-N-lyase from Flavobacterium saccharophilum IFO 13984

Kim

Joo

Kim

et al. 2011

Biotechnol Bioproc E

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In this study, we report the first functional cloning and heterogeneous expression of 3-ketovalidoxylamine C-N lyase (E.C. 4.3.3.1) from Flavobacterium saccharophilum IFO 13984. This gene is 1,098 bp in length and encodes a peptide of 366 amino acids. The recombinant C-N lyase was successfully overexpressed in E. coli, and its functional activity, degradation of 3-ketovalidoxylamine A, was confirmed by HPLC analysis. The sequence and phylogenetic analysis showed that the C-N lyase has no similarity with other amine lyases (E.C. 4.3.3) but has similarity with the conserved domain present in SusD and RagB. Thus, the C-N lyase may have a similar binding domain for sugar moieties with SusD/RagB. This genetic information may lead to improvements in C-N lyase function for industrial applications.

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Purification and characterization of the glucoside 3-dehydrogenase produced by a newly isolated Stenotrophomonas maltrophilia CCTCC M 204024

Cited by 19 publications

References 20 publications

The thuEFGKAB Operon of Rhizobia and Agrobacterium tumefaciens Codes for Transport of Trehalose, Maltitol, and Isomers of Sucrose and Their Assimilation through the Formation of Their 3-Keto Derivatives

The thuEFGKAB Operon of Rhizobia and Agrobacterium tumefaciens Codes for Transport of Trehalose, Maltitol, and Isomers of Sucrose and Their Assimilation through the Formation of Their 3-Keto Derivatives

Enhanced production of valienamine by Stenotrophomonas maltrophilia with fed-batch culture in a stirred tank bioreactor

Gene cloning and expression of a 3-ketovalidoxylamine C-N-lyase from Flavobacterium saccharophilum IFO 13984

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