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Literature summary for 1.1.1.368 extracted from

  • Loderer, C.; Morgenstern, F.; Ansorge-Schumacher, M.
    A zinc-dependent alcohol dehydrogenase (ADH) from Thauera aromatica, reducing cyclic alpha- and beta-diketones (2015), Adv. Synth. Catal., 357, 1872-1880 .
No PubMed abstract available
Search for more literature for 1.1.1.368

Cloned(Commentary)

Cloned (Comment) Organism
gene ThaADH, recombinant expression of C-terminally StrepII-tagged in Escherichia coli strain BL21(DE3) Thauera aromatica

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc-dependent enzyme, the ADH enzymes have a Rossman fold motif containing two zinc atoms per subunit. The first zinc atom is directly involved in catalysis while the second is important for the overall structure of the enzyme Thauera aromatica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+ Thauera aromatica
-
 6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Thauera aromatica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography Thauera aromatica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-cyclohexanedione + NADH + H+
-
 Thauera aromatica ? + NAD+
-
 ?
1,3-cyclopentanedione + NADH + H+
-
 Thauera aromatica ? + NAD+
-
 ?
6-hydroxycyclohex-1-ene-1-carbonyl-CoA + NAD+
-
 Thauera aromatica 6-oxocyclohex-1-ene-1-carbonyl-CoA + NADH + H+
-
 ?
additional information the enzyme exhibits a substrate specificity with highest activities on cyclic alpha- and beta-diketones including 1,2-cyclohexanedione and 1,3-cyclopentanedione, enzyme activity with 1,2-cyclohexanedione, 1,3-cyclohexanedione, and 1,3-cyclopentanedione as well as with 2,3/pentanedione, ethyl pyruvate, and cyclohexanone, but ThaADH converts neither acetophenone nor benzaldehyde which are both preferred substrates of many known zinc-dependent ADHs. The enzyme actually prefers substrates with the reactive carbonyl function being located inside a cyclohexyl or cyclopentyl structure Thauera aromatica ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 38000, SDS-PAGE Thauera aromatica

Synonyms

Synonyms Comment Organism
ThaADH
-
 Thauera aromatica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 recombinant enzyme Thauera aromatica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 recombinant enzyme Thauera aromatica

pH Range

pH Minimum pH Maximum Comment Organism
6 7 recombinant enzyme, maximal activity at pH 6.0, 40% of maximal activity at pH 7.0, and 15% at pH 5.0, profile overview Thauera aromatica

Cofactor

Cofactor Comment Organism Structure
NAD+ specific for, no activity with NADP+ Thauera aromatica

General Information

General Information Comment Organism
evolution the enzyme belongs to the zinc-dependent alcohol dehydrogenases (ADHs) Thauera aromatica
metabolism the enzyme is involved in the benzoate degradation pathway Thauera aromatica
additional information ThaADH three-dimensional structure modeling overview. A bulky aromatic residue, that plays a crucial role in the definition of the substrate binding pockets of most ADHs, is replaced by a glycine residue in ThaADH. This structural difference leads to the formation of one large binding pocket instead of two smaller ones and consequently to a preference for cyclic diketones over linear bulky substrates Thauera aromatica