1.1.1.406: galactitol 2-dehydrogenase (L-tagatose-forming)
This is an abbreviated version!
For detailed information about galactitol 2-dehydrogenase (L-tagatose-forming), go to the full flat file.
Reaction
Synonyms
galactitol dehydrogenase, GatDH, More
ECTree
1.1.1.406 galactitol 2-dehydrogenase (L-tagatose-forming)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.1.1.406 - galactitol 2-dehydrogenase (L-tagatose-forming)
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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
-
-
-
-
r
3,4-hexanedione + NADH
? + NAD+
-
-
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
-
-
?
1,2-hexanediol + NAD+
2-oxohexanol + NADH + H+
with the redox mediator 4-carboxy-2,5,7-trinitrofluorenylidenmalonnitrile, CTFM, in solute form
-
-
?
meso-erythritol + NAD+
? + NADH + H+
very low activity
-
-
r
xylitol + NAD+
L-xylulose + NADH + H+
410% of the activity with galactitol
-
-
r
xylitol + NAD+
L-xylulose + NADH + H+
410% of the activity with galactitol
-
-
r
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
?
-
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 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
-
-
?
