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1,5-anhydro-D-fructose + NADH = 1,5-anhydro-D-mannitol + NAD+
-
1,5-anhydro-D-fructose + NADP+ = 1,5-anhydro-D-mannitol + NADPH
-
1,5-anhydro-D-fructose + NADPH = 1,5-anhydro-D-glucitol + NADP+
-
1,5-anhydro-D-fructose + NADPH = 1,5-anhydro-D-mannitol + NADP+
-
1,5-anhydro-D-fructose + NADH + H+ = 1,5-anhydro-D-mannitol + NAD+
-
1,5-anhydro-D-fructose + NADPH + H+ = 1,5-anhydro-D-mannitol + NADP+
-
1,5-anhydro-D-fructose + O2 = 1,5-anhydro-3-keto-D-fructose + H2O2
-
sucrose + 1,5-anhydro-D-fructose = alpha-D-glucopyranosyl-(1,6)-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose + alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-alpha-D-glucopyranosyl-(1,6)-O-1,5-anhydro-D-fructose
-
1,5-anhydro-D-fructose = 2-hydroxy-2-(hydroxymethyl)-2H-pyran-3(6H)-one + H2O
1,5-D-anhydrofructose = microthecin
1,5-anhydro-D-fructose = 1,5-anhydro-4-deoxy-D-glycero-hex-3-en-2-ulose + H2O
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1,5-anhydro-D-mannitol + NADP+ = 1,5-anhydro-D-fructose + NADPH
-
1,5-anhydro-D-glucitol + O2 = 1,5-anhydro-D-fructose + H2O2
-
(1,4-alpha-D-glucosyl)n = 1,5-anhydro-D-fructose + (1,4-alpha-D-glucosyl)n-1
-
amylopectin = D-glucose + 1,5-anhydro-D-fructose
-
Amylopectin = Glucose + 1,5-anhydro-D-fructose
-
Maltosaccharides = Glucose + 1,5-anhydro-D-fructose
-
maltose = D-glucose + 1,5-anhydro-D-fructose
-
Maltose = Glucose + 1,5-anhydro-D-fructose
-
starch = 1,5-anhydro-D-fructose + ?
-
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1.3
-
mutant D176A in the presence of NADPH
3.7
-
mutant H108A in the presence of NADPH
4.2
-
mutant K94G in the presence of NADPH
5.5
-
mutant A13G/S10G in the presence of NADH
6.3
-
mutant A13G/S33D in the presence of NADPH
12.4
-
mutant A13G in the presence of NADH
13.5
-
mutant S33D in the presence of NADH
119
-
mutant S10G in the presence of NADPH
145
-
recombinant wild type enzyme in the presence of NADPH
156
-
mutant G206I in the presence of NADPH
216
-
native wild type enzyme in the presence of NADPH
369
-
mutant A13G/S10Gin the presence of NADPH
405
-
mutant A13G in the presence of NADPH
1.3
-
pH 7.5, mutant enzyme D176A, cofactor: NADPH
3.7
-
pH 8.0, mutant enzyme H180A, cofactor: NADPH
4.2
-
pH 6.5, mutant enzyme K94G, cofactor: NADPH
5.5
-
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH
6.3
-
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH
9.3
-
pH 7.0, 37°C, recombinant enzyme
12.4
-
pH 6.5, mutant enzyme A13G, cofactor: NADH
13.5
-
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
119
-
pH 6.5, mutant enzyme S10G, cofactor: NADPH
145
-
pH 6.5 recombinant wild-type enzyme, cofactor: NADPH
156
-
pH 6.5, mutant enzyme G206I, cofactor: NADPH
216
-
pH 6.5, native wild-type enzyme, cofactor: NADPH
369
-
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH
405
-
pH 6.5, mutant enzyme A13G, cofactor: NADPH
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1.02
-
pH 7.0, 37°C, recombinant enzyme
3.2
-
mutant A13G/S33D in the presence of NADH
3.5
-
mutant S10G in the presence of NADPH
6.4
-
recombinant wild type enzyme in the presence of NADPH
7.1
-
mutant A13G/S10Gin the presence of NADPH
8.3
-
mutant G206I in the presence of NADPH
8.3
-
native wild type enzyme in the presence of NADPH
8.5
-
mutant A13G in the presence of NADPH
8.9
-
mutant H108A in the presence of NADPH
11.1
-
mutant A13G in the presence of NADH
20.2
-
mutant A13G/S33D in the presence of NADPH
22.5
-
mutant K94G in the presence of NADPH
39
-
mutant A13G/S10G in the presence of NADH
49
-
mutant D176A in the presence of NADPH
1.02
-
pH 7.0, 37°C, recombinant enzyme
3.2
-
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH
3.5
-
pH 6.5, mutant enzyme S10G, cofactor: NADPH
6.4
-
pH 6.5 recombinant wild-type enzyme, cofactor: NADPH
7.1
-
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH
8.3
-
pH 6.5, mutant enzyme G206I, cofactor: NADPH
8.3
-
pH 6.5, native wild-type enzyme, cofactor: NADPH
8.5
-
pH 6.5, mutant enzyme A13G, cofactor: NADPH
8.9
-
pH 8.0, mutant enzyme H180A, cofactor: NADPH
11.1
-
pH 6.5, mutant enzyme A13G, cofactor: NADH
20.2
-
pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH
22.5
-
pH 6.5, mutant enzyme K94G, cofactor: NADPH
39
-
pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH
49
-
pH 7.5, mutant enzyme D176A, cofactor: NADPH
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Effects of 1,5-anhydro-D-fructose on selected glucose-metabolizing enzymes
1993
Taguchi, T.; Haruna, M.; Okuda, J.
Biotechnol. Appl. Biochem.
18
275-283
Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose
1998
Sakuma, M.; Kametani, S.; Akanuma, H.
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Increases in 1,5-anhydroglucitol levels in germinating amaranth seeds and in ripening banana
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Konishi, Y.; Hashima, K.; Kishida, K.
Biosci. Biotechnol. Biochem.
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2462-2465
Fungal pyranose oxidases: occurrence, properties and biotechnical applications in carbohydrate chemistry
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Giffhorn, F.
Appl. Microbiol. Biotechnol.
54
727-740
Characterization of exo-(1,4)-alpha glucan lyase from red alga Gracilaria chorda. Activation, inactivation and the kinetic properties of the enzyme
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Yoshinaga, K.; Fujisue, M.; Abe, J.; Hanashiro, I.; Takeda, Y.; Muroya, K.; Hizukuri, S.
Biochim. Biophys. Acta
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447-454
Enzymatic description of the anhydrofructose pathway of glycogen degradation; I. Identification and purification of anhydrofructose dehydratase, ascopyrone tautomerase and alpha-1,4-glucan lyase in the fungus Anthracobia melaloma
2004
Yu, S.; Refdahl, C.; Lundt, I.
Biochim. Biophys. Acta
1672
120-129
Enzyme kinetics and chemical modification of alpha-1,4-glucan lyase from Gracilariopsis sp.
2000
Nyvall, P.; Pedersen, M.; Kenne, L.; Gacesa, P.
Phytochemistry
54
139-145
A novel family of glucosyl 1,5-anhydro-D-fructose derivatives synthesised by transglucosylation with dextransucrase from Leuconostoc mesenteroides NRRL B-512F
2005
Richard, G.; Yu, S.; Monsan, P.; Remaud-Simeon, M.; Morel, S.
Carbohydr. Res.
340
395-401
Catabolism of 1,5-anhydro-D-fructose in Sinorhizobium morelense S-30.7.5: discovery, characterization, and overexpression of a new 1,5-anhydro-D-fructose reductase and its application in sugar analysis and rare sugar synthesis
2006
Kuehn, A.; Yu, S.; Giffhorn, F.
Appl. Environ. Microbiol.
72
1248-1257
Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis
2006
Dambe, T.R.; Kuehn, A.M.; Brossette, T.; Giffhorn, F.; Scheidig, A.J.
Biochemistry
45
10030-10042
Enzymatic description of the anhydrofructose pathway of glycogen degradation II. Gene identification and characterization of the reactions catalyzed by aldos-2-ulose dehydratase that converts 1,5-anhydro-D-fructose to microthecin with ascopyrone M as the intermediate
2005
Yu, S.
Biochim. Biophys. Acta
1723
63-73
The anhydrofructose pathway and its possible role in stress response and signaling
2006
Yu, S.; Fiskesund, R.
Biochim. Biophys. Acta
1760
1314-1322
-
Presence of microthecin in the red alga Gracilariopsis lemaneiformis and its formation from 1,5-anhydro-D-fructose
1996
Broberg, A.; Kenne, L.; Pedersen, M.
Phytochemistry
41
151-154
Mouse AKR1E1 is an ortholog of pig liver NADPH dependent 1,5-anhydro-D-fructose reductase
2008
Sakuma, M.; Kubota, S.
Biosci. Biotechnol. Biochem.
72
872-876
-
Enzymatic production of microthecin by aldos-2-ulose dehydratase from 1,5-anhydro-D-fructose and stability studies of microthecin
2008
Yu, S.; Andreassen, M.; Lundt, I.
Biocatal. Biotransform.
26
169-176
1,5-Anhydro-D-fructose: biocatalytic and chemical synthetic methods for the preparation, transformation and derivatization
2010
Lundt, I.; Yu, S.
Carbohydr. Res.
345
181-190
Crystal structure of bifunctional aldos-2-ulose dehydratase/isomerase from Phanerochaete chrysosporium with the reaction intermediate ascopyrone M
2012
Claesson, M.; Lindqvist, Y.; Madrid, S.; Sandalova, T.; Fiskesund, R.; Yu, S.; Schneider, G.
J. Mol. Biol.
417
279-293
Foreign peptide triggers boost in pneumococcal metabolism and growth
2018
Nasher, F.; Foerster, S.; Yildirim, E.; Grandgirard, D.; Leib, S.; Heller, M.; Hathaway, L.
BMC Microbiol.
18
23
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