Enzymes
UniProtKB help_outline | 1 proteins |
Enzyme class help_outline |
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Name help_outline
a ubiquinone
Identifier
CHEBI:16389
(CAS: 1339-63-5)
help_outline
Charge
0
Formula
C9H10O4(C5H8)n
Search links
Involved in 49 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9565Polymer name: a ubiquinonePolymerization index help_outline nFormula C9H10O4(C5H8)nCharge (0)(0)nMol File for the polymer
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- Name help_outline keto-D-fructose Identifier CHEBI:48095 (Beilstein: 5732297,1239004; CAS: 57-48-7) help_outline Charge 0 Formula C6H12O6 InChIKeyhelp_outline BJHIKXHVCXFQLS-UYFOZJQFSA-N SMILEShelp_outline OC[C@@H](O)[C@@H](O)[C@H](O)C(=O)CO 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 5-dehydro-D-fructose Identifier CHEBI:17011 (CAS: 1684-29-3) help_outline Charge 0 Formula C6H10O6 InChIKeyhelp_outline AWQIYVPBMVSGCL-PHDIDXHHSA-N SMILEShelp_outline OCC(=O)[C@@H](O)[C@H](O)C(=O)CO 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
a ubiquinol
Identifier
CHEBI:17976
(CAS: 56275-39-9)
help_outline
Charge
0
Formula
C9H12O4(C5H8)n
Search links
Involved in 55 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:9566Polymer name: a ubiquinolPolymerization index help_outline nFormula C9H12O4(C5H8)nCharge (0)(0)nMol File for the polymer
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Cross-references
RHEA:22304 | RHEA:22305 | RHEA:22306 | RHEA:22307 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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D-fructose dehydrogenase of Gluconobacter industrius: purification, characterization, and application to enzymatic microdetermination of D-fructose.
Ameyama M., Shinagawa E., Matsushita K., Adachi O.
D-Fructose dehydrogenase was solubilized and purified from the membrane fraction of glycerol-grown Gluconobacter industrius IFO 3260 by a procedure involving solubilization of the enzyme with Triton X-100 and subsequent fractionation on diethylaminoethyl-cellulose and hydroxylapatite columns. The ... >> More
D-Fructose dehydrogenase was solubilized and purified from the membrane fraction of glycerol-grown Gluconobacter industrius IFO 3260 by a procedure involving solubilization of the enzyme with Triton X-100 and subsequent fractionation on diethylaminoethyl-cellulose and hydroxylapatite columns. The purified enzyme was tightly bound to a c-type cytochrome and another peptide existing as a dehydrogenase-cytochrome complex. The purified enzyme was deemed pure by analytical ultracentrifugation as well as by gel filtration on a Sephadex G-200 column. The molecular weight of the enzyme complex was determined to be about 140,000, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed the presence of three components having molecular weights of 67,000 (dehydrogenase), 50,800 (cytochrome c), and 19,700 (unknown function). Only D-fructose was readily oxidized by the enzyme in the presence of dyes such as ferricyanide, 2,6-dichlorophenolindophenol, or phenazine methosulfate. Nicotinamide adenine dinucleotide, nicotinamide adenine dinucleotide phosphate, and oxygen did not function as electron acceptors. The optimum pH of D-fructose oxidation was 4.0. The enzyme was stable at pH 4.5 to 6.0 Stability of the purified enzyme was much enhanced by the presence of detergent in the enzyme solution. Removal of detergent from the enzyme solution facilitated the aggregation of the enzyme and caused its inactivation. An apparent Michaelis constant for D-fructose was observed to be 10(-2) M with the purified enzyme. D-Fructose dehydrogenase was shown to be a satisfactory reagent for microdetermination of D-fructose. << Less
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Enzymatic studies on the oxidation of sugar and sugar alcohol. I. Purification and properties of particle-bound fructose dehydrogenase.
Yamada Y., Aida K., Uemura T.
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Kinetic studies of the active sites functioning in the quinohemoprotein fructose dehydrogenase.
Marcinkeviciene J., Johansson G.
Steady-state kinetic analysis was performed on the reaction between D-fructose and ferricyanide with the quinohemoprotein fructose dehydrogenase from Gluconobacter species. The D-fructose oxidation dependence on the ferricyanide concentration resulted in a series of parallel reciprocal plots, and ... >> More
Steady-state kinetic analysis was performed on the reaction between D-fructose and ferricyanide with the quinohemoprotein fructose dehydrogenase from Gluconobacter species. The D-fructose oxidation dependence on the ferricyanide concentration resulted in a series of parallel reciprocal plots, and the reaction was assumed to proceed by a ping-pong type of mechanism. A reciprocal plot of the reduction of ferricyanide at saturating concentration of D-fructose gave a break which was considered to appear as a result of the two active centers, namely PQQ and heme c functioning. A scheme of action is proposed and the bimolecular rate constant of the D-fructose oxidation, the kcat for PQQ and the electron transfer rate between the PQQH2 and heme c are calculated and account for 2.2 +/- 0.4 x 10(4) M-1 s-1, (93 +/- 14) and (162 +/-7) s-1, respectively. << Less
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Heterologous overexpression and characterization of a flavoprotein-cytochrome c complex fructose dehydrogenase of Gluconobacter japonicus NBRC3260.
Kawai S., Goda-Tsutsumi M., Yakushi T., Kano K., Matsushita K.
A heterotrimeric flavoprotein-cytochrome c complex fructose dehydrogenase (FDH) of Gluconobacter japonicus NBRC3260 catalyzes the oxidation of d-fructose to produce 5-keto-d-fructose and is used for diagnosis and basic research purposes as a direct electron transfer-type bioelectrocatalysis. The f ... >> More
A heterotrimeric flavoprotein-cytochrome c complex fructose dehydrogenase (FDH) of Gluconobacter japonicus NBRC3260 catalyzes the oxidation of d-fructose to produce 5-keto-d-fructose and is used for diagnosis and basic research purposes as a direct electron transfer-type bioelectrocatalysis. The fdhSCL genes encoding the FDH complex of G. japonicus NBRC3260 were isolated by a PCR-based gene amplification method with degenerate primers designed from the amino-terminal amino acid sequence of the large subunit and sequenced. Three open reading frames for fdhSCL encoding the small, cytochrome c, and large subunits, respectively, were found and were presumably in a polycistronic transcriptional unit. Heterologous overexpression of fdhSCL was conducted using a broad-host-range plasmid vector, pBBR1MCS-4, carrying a DNA fragment containing the putative promoter region of the membrane-bound alcohol dehydrogenase gene of Gluconobacter oxydans and a G. oxydans strain as the expression host. We also constructed derivatives modified in the translational initiation codon to ATG from TTG, designated (TTG)FDH and (ATG)FDH. Membranes of the cells producing recombinant (TTG)FDH and (ATG)FDH showed approximately 20 times and 100 times higher specific activity than those of G. japonicus NBRC3260, respectively. The cells producing only FdhS and FdhL had no fructose-oxidizing activity, but showed significantly high d-fructose:ferricyanide oxidoreductase activity in the soluble fraction of cell extracts, whereas the cells producing the FDH complex showed activity in the membrane fraction. It is reasonable to conclude that the cytochrome c subunit is responsible not only for membrane anchoring but also for ubiquinone reduction. << Less
Appl. Environ. Microbiol. 79:1654-1660(2013) [PubMed] [EuropePMC]