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Information on EC 1.1.1.406 - galactitol 2-dehydrogenase (L-tagatose-forming)
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1.1.1.406 galactitol 2-dehydrogenase (L-tagatose-forming)IUBMB Comments
The enzyme, characterized in the bacterium Rhodobacter sphaeroides, has a wide subtrate specificity. In addition to galactitol, it primarily oxidizes D-threitol and xylitol, and in addition to L-tagatose, it primarily reduces L-erythrulose, D-ribulose and L-glyceraldehyde. It is specific for NAD+. The enzyme also shows activity with D-tagatose (cf. EC 1.1.1.16, galactitol 2-dehydrogenase).
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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Synonyms
gatdh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
galactitol dehydrogenase
GatDH
additional information
GatDH
-
-
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-
additional information
GatDH belongs to the protein superfamily of short-chain dehydrogenases
additional information
GatDH belongs to the protein superfamily of short-chain dehydrogenases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
galactitol + NAD+ = L-tagatose + NADH + H+
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-
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galactitol + NAD+ = D-tagatose + NADH + H+
reaction mechanism, overview
galactitol + NAD+ = D-tagatose + NADH + H+
reaction mechanism, overview
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galactitol + NAD+ = D-tagatose + NADH + H+
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SYSTEMATIC NAME
IUBMB Comments
galactitol:NAD+ 2-oxidoreductase (L-tagatose-forming)
The enzyme, characterized in the bacterium Rhodobacter sphaeroides, has a wide subtrate specificity. In addition to galactitol, it primarily oxidizes D-threitol and xylitol, and in addition to L-tagatose, it primarily reduces L-erythrulose, D-ribulose and L-glyceraldehyde. It is specific for NAD+. The enzyme also shows activity with D-tagatose (cf. EC 1.1.1.16, galactitol 2-dehydrogenase).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-1,2,6-hexanetriol + NAD+
1,6-dihydroxy-2-hexanone + NADH
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-
-
-
r
3,4-hexanedione + NADH
? + NAD+
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-
reaction product is a complex polymer
-
r
1,2-hexanediol + NAD+
2-oxohexanol + NADH + H+
with the redox mediator 4-carboxy-2,5,7-trinitrofluorenylidenmalonnitrile, CTFM, in solute form
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-
?
1,2-hexanediol + NAD+
2-oxohexanol + NADH + H+
with the redox mediator 4-carboxy-2,5,7-trinitrofluorenylidenmalonnitrile, CTFM, in solute form
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-
?
meso-erythritol + NAD+
? + NADH + H+
very low activity
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-
r
xylitol + NAD+
L-xylulose + NADH + H+
410% of the activity with galactitol
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-
r
xylitol + NAD+
L-xylulose + NADH + H+
410% of the activity with galactitol
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-
r
additional information
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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-
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
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-
?
additional information
?
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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
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-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Mg2+
additional information
activity of GatDH is strictly dependent on the presence of divalent metal ions
Mg2+
GatDH constitutes a homotetramer with two magnesium-ion binding sites each formed by two opposing C termini, binding site structure, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-dipyridyl
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13% inhibition at 1 mM, restored by addition of 2 mM MgCl2
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
22
galactitol
pH not specified in the publication, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, free or with bound 1,2-pentanediol or meso-erythritol, hanging drop vapour diffusion method, 0.001 ml of 0.45 mM protein with 1 mM NAD+ or NADH, in 20 mM Bis-Tris, pH 6.5, is mixed with 0.001 ml of reservoir solution containing 100 mM MES, pH 5.5-5.9, 200 mM MgCl2, and 10-20% w/v methoxy poly(ethylene glycol), equilibration against 1 ml reservoir solution, 1 week, X-ray diffraction structure determnination and analysis at 1.25-195 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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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
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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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 20 mM Bis-Tris, pH 6.5, 1 mM MgCl2, 30% sucrose, stable for 3 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His(6)-tagged GatDH from Escherichia coli strain BL21GOLD(DE3) by use of Co2+-IDA functionalized Fe2O3 nanoparticles, purification and immobilization method, overview
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His6-tagged GatDH from Escherichia coli strain BL21(DE3), by nickel affinity chromatography the tag is cleaved off, followed by dialysis and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression of His6-tagged GatDH in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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Release 2023.1 (January 2023)
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