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Literature summary for 3.7.1.11 extracted from

  • Loschonsky, S.; Waltzer, S.; Fraas, S.; Wacker, T.; Andrade, S.L.; Kroneck, P.M.; Mueller, M.
    Catalytic scope of the thiamine-dependent multifunctional enzyme cyclohexane-1,2-dione hydrolase (2014), ChemBioChem, 15, 389-392.
    View publication on PubMed
Search for more literature for 3.7.1.11

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Azoarcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cyclohexane-1,2-dione + H2O Azoarcus sp.
-
 6-oxohexanoate
-
 ?
cyclohexane-1,2-dione + H2O Azoarcus sp. 22Lin
-
 6-oxohexanoate
-
 ?
additional information Azoarcus sp. the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid ?
-
 ?
additional information Azoarcus sp. 22Lin the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid ?
-
 ?

Organism

Organism UniProt Comment Textmining
Azoarcus sp. P0CH62
-
-
Azoarcus sp. 22Lin P0CH62
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Azoarcus sp.

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:cyclohexane-1,2-diol-grown cell cyclohexane-1,2-diol as the sole carbon source and electron donor, and nitrate as electron acceptor Azoarcus sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cyclohexane-1,2-dione + H2O
-
 Azoarcus sp. 6-oxohexanoate
-
 ?
cyclohexane-1,2-dione + H2O
-
 Azoarcus sp. 22Lin 6-oxohexanoate
-
 ?
additional information the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid Azoarcus sp. ?
-
 ?
additional information determination of the catalytic activity of recombinant enzyme CDH, both cleavage of cyclohexane-1,2-dione and the cross-benzoin reaction of benzaldehyde and pyruvate. The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) is performed on an analytical scale. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields Azoarcus sp. ?
-
 ?
additional information the enzyme catalyzes C-C bond cleavage of cyclohexane-1,2-dione to produce 6-oxohexanoic acid as the primary product, presumably followed by oxidation of the latter to adipic acid Azoarcus sp. 22Lin ?
-
 ?
additional information determination of the catalytic activity of recombinant enzyme CDH, both cleavage of cyclohexane-1,2-dione and the cross-benzoin reaction of benzaldehyde and pyruvate. The enzyme is able to catalyze nonphysiological asymmetric C-C bond formation, the cross-benzoin reaction of benzaldehyde and pyruvate (after decarboxylation) to result in the R-configured 1-hydroxy-1-phenylpropan-2-one (98% ee) is performed on an analytical scale. The recombinant CDH shows the same C-C bond-cleavage and C-C bond-formation activity as the enzyme purified from its native source, Azoarcus sp. strain 22Lin. Enzyme CDH catalyzes the asymmetric cross-benzoin reaction of aromatic aldehydes and (decarboxylated) pyruvate (up to quantitative conversion, 92-99% ee). The enzyme accepts also hydroxybenzaldehydes and nitrobenzaldehydes. On a semipreparative scale, sterically demanding 4-(tert-butyl)benzaldehyde and 2-naphthaldehyde are transformed into the corresponding 2-hydroxy ketone products in high yields Azoarcus sp. 22Lin ?
-
 ?

Subunits

Subunits Comment Organism
homodimer the enzyme is a homodimer in solution, the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer Azoarcus sp.

Synonyms

Synonyms Comment Organism
Cdh
-
 Azoarcus sp.

Cofactor

Cofactor Comment Organism Structure
FAD noncovalently bound, one FAD per monomer Azoarcus sp.
additional information the crystal structure shows a homotetramer with one noncovalently bound FAD and one thiamine diphosphate per monomer Azoarcus sp.
thiamine diphosphate dependent on, one thiamine diphosphate per monomer Azoarcus sp.

General Information

General Information Comment Organism
physiological function thiamine diphosphate-dependent cyclohexane-1,2-dione hydrolase is the key enzyme of an anaerobic degradation pathway of alicyclic alcohols Azoarcus sp.