Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.406 extracted from

  • 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 (2009), Langmuir, 25, 12380-12386.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Cereibacter sphaeroides

Protein Variants

Protein Variants Comment Organism
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 Cereibacter sphaeroides

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Cereibacter sphaeroides

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26385
-
4 * 26385, amino acid sequence calculation Cereibacter sphaeroides
110000
-
-
Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides C0KTJ6
-
-
Cereibacter sphaeroides D C0KTJ6
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Cereibacter sphaeroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-hexanediol + NAD+ with the redox mediator 4-carboxy-2,5,7-trinitrofluorenylidenmalonnitrile, CTFM, in solute form Cereibacter sphaeroides 2-oxohexanol + NADH + H+
-
?
1,2-hexanediol + NAD+ with the redox mediator 4-carboxy-2,5,7-trinitrofluorenylidenmalonnitrile, CTFM, in solute form Cereibacter sphaeroides D 2-oxohexanol + NADH + H+
-
?
galactitol + NAD+
-
Cereibacter sphaeroides L-tagatose + NADH + H+
-
r
galactitol + NAD+
-
Cereibacter sphaeroides D L-tagatose + NADH + H+
-
r
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 Cereibacter sphaeroides ?
-
?
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 Cereibacter sphaeroides D ?
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 26385, amino acid sequence calculation Cereibacter sphaeroides

Synonyms

Synonyms Comment Organism
galactitol dehydrogenase
-
Cereibacter sphaeroides
GatDH
-
Cereibacter sphaeroides

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Cereibacter sphaeroides

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
assay at Cereibacter sphaeroides

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Cereibacter sphaeroides
NADH
-
Cereibacter sphaeroides