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(2R)-butanol + NAD+
2-butanone + NADH
-
Substrates: -
Products: -
?
(2S)-butanol + NAD+
2-butanone + NADH
-
Substrates: -
Products: -
?
(2S,3S)-butanediol + NAD+
? + NADH
-
Substrates: -
Products: -
?
(S)-1,2,6-hexanetriol + NAD+
1,6-dihydroxy-2-hexanone + NADH
-
Substrates: -
Products: -
r
(S)-1,2-butanediol + NAD+
1-hydroxy-2-butanone + NADH
-
Substrates: -
Products: -
r
(S)-1,2-hexanediol + NAD+
1-hydroxy-2-hexanone + NADH
-
Substrates: -
Products: -
r
(S)-1,2-propanediol + NAD+
hydroxyacetone + NADH
-
Substrates: -
Products: -
r
1,2-(S)-pentanediol + NAD+
? + NADH + H+
Substrates: -
Products: -
r
1,2-butanediol + NAD+
? + NADH
-
Substrates: -
Products: -
?
1,2-hexanediol + NAD+
2-oxohexanol + NADH + H+
1,2-hexanediol + NAD+
? + NADH
-
Substrates: -
Products: -
?
1,2-pentanediol + NAD+
? + NADH
-
Substrates: -
Products: -
?
1,2-propanediol + NAD+
? + NADH
-
Substrates: -
Products: -
?
1-hydroxy-2-butanone + NADH
(S)-1,2-butanediol + NAD+
-
Substrates: -
Products: -
r
2,3-hexandione + NADH
(2R,3S)-hexanediol + NAD+
-
Substrates: -
Products: -
r
2-hexanol + NAD+
2-hexanone + NADH
-
Substrates: -
Products: -
?
2-propanol + NAD+
acetone + NADH
-
Substrates: -
Products: -
?
3,4-hexanedione + NADH
? + NAD+
-
Substrates: -
Products: reaction product is a complex polymer
r
acetoin + NADH
? + NAD+
-
Substrates: -
Products: -
?
D-arabitol + NAD+
? + NADH
-
Substrates: -
Products: -
?
D-ribulose + NADH
? + NAD+
-
Substrates: -
Products: -
?
D-threitol + NAD+
? + NADH
-
Substrates: best substrate tested
Products: -
?
D-xylulose + NADH
? + NAD+
-
Substrates: -
Products: -
?
dihydroxyacetone + NADH
? + NAD+
-
Substrates: -
Products: -
?
galactitol + NAD+
L-tagatose + NADH
-
Substrates: -
Products: -
r
galactitol + NAD+
L-tagatose + NADH + H+
glycerol + NAD+
DL-glyceraldehyde + NADH
-
Substrates: -
Products: -
r
hydroxyacetone + NADH
(S)-1,2-propanediol + NAD+
-
Substrates: -
Products: -
r
L-erythrulose + NADH
? + NAD+
-
Substrates: -
Products: -
?
L-glucitol + NAD+
? + NADH
-
Substrates: -
Products: -
?
meso-erythritol + NAD+
? + NADH + H+
xylitol + NAD+
L-xylulose + NADH + H+
additional information
?
-
1,2-hexanediol + NAD+
2-oxohexanol + NADH + H+
Substrates: with the redox mediator 4-carboxy-2,5,7-trinitrofluorenylidenmalonnitrile, CTFM, in solute form
Products: -
?
1,2-hexanediol + NAD+
2-oxohexanol + NADH + H+
Substrates: with the redox mediator 4-carboxy-2,5,7-trinitrofluorenylidenmalonnitrile, CTFM, in solute form
Products: -
?
galactitol + NAD+
L-tagatose + NADH + H+
Substrates: -
Products: -
?
galactitol + NAD+
L-tagatose + NADH + H+
Substrates: -
Products: -
r
galactitol + NAD+
L-tagatose + NADH + H+
-
Substrates: -
Products: -
r
galactitol + NAD+
L-tagatose + NADH + H+
Substrates: -
Products: -
r
meso-erythritol + NAD+
? + NADH + H+
Substrates: very low activity
Products: -
r
meso-erythritol + NAD+
? + NADH + H+
Substrates: very low activity
Products: -
r
xylitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
L-xylulose + NADH + H+
-
Substrates: high activity
Products: -
r
xylitol + NAD+
L-xylulose + NADH + H+
Substrates: 410% of the activity with galactitol
Products: -
r
xylitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
L-xylulose + NADH + H+
Substrates: 410% of the activity with galactitol
Products: -
r
additional information
?
-
Substrates: GatDH catalyzes the dehydrogenation of a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction it reduces prochiral ketones with high stereoselectivity yielding the corresponding S-configured secondary alcohols
Products: -
?
additional information
?
-
Substrates: GatDH from Rhodobacter sphaeroides is a multifunctional enzyme that catalyzes in the presence of oxidized beta-NAD+ the interconversion of various multivalent aliphatic alcohols to the corresponding ketone. GatDH oxidizes a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction, it reduces ketones with high stereoselectivity yielding the corresponding S-configurated alcohols
Products: -
?
additional information
?
-
-
Substrates: GatDH from Rhodobacter sphaeroides is a multifunctional enzyme that catalyzes in the presence of oxidized beta-NAD+ the interconversion of various multivalent aliphatic alcohols to the corresponding ketone. GatDH oxidizes a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction, it reduces ketones with high stereoselectivity yielding the corresponding S-configurated alcohols
Products: -
?
additional information
?
-
Substrates: site mapping, the catalytic tetrad is formed by Asn116, Ser144, Tyr159, and Lys163. The substrate binding pocket can be divided into two parts of different size and polarity. In the smaller part, the side chains of amino acids Ser144, Ser146, and Asn151 are important determinants for the binding specificity and the orientation of (pro-) chiral compounds. The larger part of the pocket is elongated and flanked by polar and non-polar residues, enabling a rather broad substrate spectrum. NAD(H) binding structure, overview
Products: -
?
additional information
?
-
Substrates: GatDH catalyzes the dehydrogenation of a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction it reduces prochiral ketones with high stereoselectivity yielding the corresponding S-configured secondary alcohols
Products: -
?
additional information
?
-
Substrates: site mapping, the catalytic tetrad is formed by Asn116, Ser144, Tyr159, and Lys163. The substrate binding pocket can be divided into two parts of different size and polarity. In the smaller part, the side chains of amino acids Ser144, Ser146, and Asn151 are important determinants for the binding specificity and the orientation of (pro-) chiral compounds. The larger part of the pocket is elongated and flanked by polar and non-polar residues, enabling a rather broad substrate spectrum. NAD(H) binding structure, overview
Products: -
?
additional information
?
-
Substrates: GatDH from Rhodobacter sphaeroides is a multifunctional enzyme that catalyzes in the presence of oxidized beta-NAD+ the interconversion of various multivalent aliphatic alcohols to the corresponding ketone. GatDH oxidizes a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction, it reduces ketones with high stereoselectivity yielding the corresponding S-configurated alcohols
Products: -
?
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D-arabitol + NAD+
? + NADH
-
Substrates: -
Products: -
?
D-ribulose + NADH
? + NAD+
-
Substrates: -
Products: -
?
D-threitol + NAD+
? + NADH
-
Substrates: best substrate tested
Products: -
?
D-xylulose + NADH
? + NAD+
-
Substrates: -
Products: -
?
galactitol + NAD+
L-tagatose + NADH
-
Substrates: -
Products: -
r
galactitol + NAD+
L-tagatose + NADH + H+
L-erythrulose + NADH
? + NAD+
-
Substrates: -
Products: -
?
L-glucitol + NAD+
? + NADH
-
Substrates: -
Products: -
?
xylitol + NAD+
L-xylulose + NADH + H+
additional information
?
-
galactitol + NAD+
L-tagatose + NADH + H+
Substrates: -
Products: -
?
galactitol + NAD+
L-tagatose + NADH + H+
Substrates: -
Products: -
r
galactitol + NAD+
L-tagatose + NADH + H+
-
Substrates: -
Products: -
r
galactitol + NAD+
L-tagatose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
r
xylitol + NAD+
L-xylulose + NADH + H+
-
Substrates: high activity
Products: -
r
xylitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
r
additional information
?
-
Substrates: GatDH catalyzes the dehydrogenation of a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction it reduces prochiral ketones with high stereoselectivity yielding the corresponding S-configured secondary alcohols
Products: -
?
additional information
?
-
Substrates: GatDH from Rhodobacter sphaeroides is a multifunctional enzyme that catalyzes in the presence of oxidized beta-NAD+ the interconversion of various multivalent aliphatic alcohols to the corresponding ketone. GatDH oxidizes a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction, it reduces ketones with high stereoselectivity yielding the corresponding S-configurated alcohols
Products: -
?
additional information
?
-
-
Substrates: GatDH from Rhodobacter sphaeroides is a multifunctional enzyme that catalyzes in the presence of oxidized beta-NAD+ the interconversion of various multivalent aliphatic alcohols to the corresponding ketone. GatDH oxidizes a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction, it reduces ketones with high stereoselectivity yielding the corresponding S-configurated alcohols
Products: -
?
additional information
?
-
Substrates: GatDH catalyzes the dehydrogenation of a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction it reduces prochiral ketones with high stereoselectivity yielding the corresponding S-configured secondary alcohols
Products: -
?
additional information
?
-
Substrates: GatDH from Rhodobacter sphaeroides is a multifunctional enzyme that catalyzes in the presence of oxidized beta-NAD+ the interconversion of various multivalent aliphatic alcohols to the corresponding ketone. GatDH oxidizes a variety of polyvalent aliphatic alcohols and polyols to the corresponding ketones and ketoses, respectively, and in the reverse reaction, it reduces ketones with high stereoselectivity yielding the corresponding S-configurated alcohols
Products: -
?
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additional information
directed functional immobilization of the enzyme on gold surfaces, representing a proof-of-concept for the development of reactors for electrochemical synthon preparation using dehydrogenases, method development and evaluation, overview
additional information
-
directed functional immobilization of the enzyme on gold surfaces, representing a proof-of-concept for the development of reactors for electrochemical synthon preparation using dehydrogenases, method development and evaluation, overview
additional information
rapid immobilization with the one-pot purification of galactitol dehydrogenase and formate dehydrogenase, using iminodiacetic acid with chelated Co2+ modified magnetic nanoparticles as a carrier, for (S)-1,2-propanediol and L-tagatose production. Lactate dehydrogenase from recombinant Escherichia coli and formate dehydrogenase from Candida methylica are used for the regeneration of NADH/NAD+ with a representative synthesis of (S)-1,2-propanediol and L-tagatose starting from hydroxyacetone and galactitol, overview. The immobilized enzyme system retained up to 70% of its activity after one week of repeated use. One-pot purification of His6-tagged GatDH and FDH followed by the production of rare sugar and chiral diol by use of affinity magnetic nanoparticles
additional information
-
directed functional immobilization of the enzyme on gold surfaces, representing a proof-of-concept for the development of reactors for electrochemical synthon preparation using dehydrogenases, method development and evaluation, overview
-
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synthesis
-
preparation of optically pure aliphatic diols by enzymic oxidation of one enantiomer or stereospecific reduction of keto-alcohols or diketones
synthesis
as an enzyme capable of the stereo- and regioselective modification of carbohydrates, GatDH exhibits a high potential for application in biotechnology as a biocatalyst, e.g. preparation of several (R)-1,2-diols by racemic resolution with GatDH as well as the synthesis of several S-configured aliphatic alcohols by reducing corresponding prochiral ketones
synthesis
synthesis of (S)-1,2-propanediol and L-tagatose starting from hydroxyacetone and galactitol using an immobilized enzyme system. One-pot purification of His6-tagged GatDH and FDH followed by the production of rare sugar and chiral diol by use of affinity magnetic nanoparticles
synthesis
galactitol dehydrogenase is coupled with water-forming NADH oxidase for efficient enzymatic synthesis of L-tagatose (a building block in the production of many value-added chemicals)
synthesis
-
the two oxidoreductases, xylose reductase and galactitol dehydrogenase are functionally expressed in the engineered yeast (EJ2g_pXpG) and enable direct production of tagatose from lactose. The expression levels of the enzymes are adjusted to maximize tagatose production. The resulting engineered yeast produces 37.69 g/L of tagatose from lactose with a tagatose and galactose ratio of 9:1 in the reaction broth
synthesis
-
as an enzyme capable of the stereo- and regioselective modification of carbohydrates, GatDH exhibits a high potential for application in biotechnology as a biocatalyst, e.g. preparation of several (R)-1,2-diols by racemic resolution with GatDH as well as the synthesis of several S-configured aliphatic alcohols by reducing corresponding prochiral ketones
-
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Schneider, K.H.; Jkel, G.; Hoffmann, R.; Giffhorn, F.
Enzyme evolution in Rhodobacter sphaeroides: Selection of a mutant expressing a new galactitol dehydrogenase and biochemical characterization of the enzyme
Microbiology
141
1865-1873
1995
Cereibacter sphaeroides
brenda
Kohring, G.W.; Wiehr, P.; Jeworski, M.; Giffhorn, F.
Stereoselective oxidation of aliphatic diols and reduction of hydroxy-ketones with galactitol dehydrogenase from Rhodobacter sphaeroides D
Commun. Agric. Appl. Biol. Sci.
68
309-312
2003
Cereibacter sphaeroides
brenda
Carius, Y.; Christian, H.; Faust, A.; Zander, U.; Klink, B.U.; Kornberger, P.; Kohring, G.W.; Giffhorn, F.; Scheidig, A.J.
Structural insight into substrate differentiation of the sugar-metabolizing enzyme galactitol dehydrogenase from Rhodobacter sphaeroides D
J. Biol. Chem.
285
20006-20014
2010
Cereibacter sphaeroides (C0KTJ6), Cereibacter sphaeroides D (C0KTJ6)
brenda
Kornberger, P.; Gajdzik, J.; Natter, H.; Wenz, G.; Giffhorn, F.; Kohring, G.W.; Hempelmann, R.
Modification of galactitol dehydrogenase from Rhodobacter sphaeroides D for immobilization on polycrystalline gold surfaces
Langmuir
25
12380-12386
2009
Cereibacter sphaeroides (C0KTJ6), Cereibacter sphaeroides, Cereibacter sphaeroides D (C0KTJ6)
brenda
Demir, A.S.; Talpur, F.N.; Betul Sopaci, S.; Kohring, G.W.; Celik, A.
Selective oxidation and reduction reactions with cofactor regeneration mediated by galactitol-, lactate-, and formate dehydrogenases immobilized on magnetic nanoparticles
J. Biotechnol.
152
176-183
2011
Cereibacter sphaeroides (C0KTJ6)
brenda
Liu, J.J.; Zhang, G.C.; Kwak, S.; Oh, E.J.; Yun, E.J.; Chomvong, K.; Cate, J.H.D.; Jin, Y.S.
Overcoming the thermodynamic equilibrium of an isomerization reaction through oxidoreductive reactions for biotransformation
Nat. Commun.
10
1356
2019
Rhizobium leguminosarum
brenda
Su, W.B.; Li, F.L.; Li, X.Y.; Fan, X.M.; Liu, R.J.; Zhang, Y.W.
Using galactitol dehydrogenase coupled with water-forming NADH oxidase for efficient enzymatic synthesis of L-tagatose
New Biotechnol.
62
18-25
2021
Cereibacter sphaeroides (C0KTJ6)
brenda