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Literature summary extracted from

  • 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 (2010), J. Biol. Chem., 285, 20006-20014.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.1.1.406 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 Cereibacter sphaeroides

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.406 expression of His6-tagged GatDH in Escherichia coli strain BL21(DE3) Cereibacter sphaeroides

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.406 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 Cereibacter sphaeroides

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.406 22
-
 galactitol pH not specified in the publication, temperature not specified in the publication Cereibacter sphaeroides

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.406 Co2+ can replace Mg2+ Cereibacter sphaeroides
1.1.1.406 Mg2+ GatDH constitutes a homotetramer with two magnesium-ion binding sites each formed by two opposing C termini, binding site structure, overview Cereibacter sphaeroides
1.1.1.406 additional information activity of GatDH is strictly dependent on the presence of divalent metal ions Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.406 galactitol + NAD+ Cereibacter sphaeroides
-
 L-tagatose + NADH + H+
-
 r
1.1.1.406 additional information Cereibacter sphaeroides 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 ?
-
 ?
1.1.1.406 additional information Cereibacter sphaeroides D 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 ?
-
 ?
1.1.1.406 xylitol + NAD+ Cereibacter sphaeroides
-
 L-xylulose + NADH + H+
-
 r
1.1.1.406 xylitol + NAD+ Cereibacter sphaeroides D
-
 L-xylulose + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.406 Cereibacter sphaeroides C0KTJ6
-
-
1.1.1.406 Cereibacter sphaeroides D C0KTJ6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.406 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 Cereibacter sphaeroides

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.406 galactitol + NAD+ = D-tagatose + NADH + H+ reaction mechanism, overview Cereibacter sphaeroides
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.406 1,2-(S)-pentanediol + NAD+
-
 Cereibacter sphaeroides ? + NADH + H+
-
 r
1.1.1.406 galactitol + NAD+
-
 Cereibacter sphaeroides L-tagatose + NADH + H+
-
 r
1.1.1.406 meso-erythritol + NAD+ very low activity Cereibacter sphaeroides ? + NADH + H+
-
 r
1.1.1.406 meso-erythritol + NAD+ very low activity Cereibacter sphaeroides D ? + NADH + H+
-
 r
1.1.1.406 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 Cereibacter sphaeroides ?
-
 ?
1.1.1.406 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 Cereibacter sphaeroides ?
-
 ?
1.1.1.406 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 Cereibacter sphaeroides D ?
-
 ?
1.1.1.406 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 Cereibacter sphaeroides D ?
-
 ?
1.1.1.406 xylitol + NAD+
-
 Cereibacter sphaeroides L-xylulose + NADH + H+
-
 r
1.1.1.406 xylitol + NAD+ 410% of the activity with galactitol Cereibacter sphaeroides L-xylulose + NADH + H+
-
 r
1.1.1.406 xylitol + NAD+
-
 Cereibacter sphaeroides D L-xylulose + NADH + H+
-
 r
1.1.1.406 xylitol + NAD+ 410% of the activity with galactitol Cereibacter sphaeroides D L-xylulose + NADH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.406 homotetramer
-
 Cereibacter sphaeroides

Synonyms

EC Number Synonyms Comment Organism
1.1.1.406 GatDH
-
 Cereibacter sphaeroides
1.1.1.406 More GatDH belongs to the protein superfamily of short-chain dehydrogenases Cereibacter sphaeroides

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.406 NAD+
-
 Cereibacter sphaeroides
1.1.1.406 NADH
-
 Cereibacter sphaeroides