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PDBsum entry 4d5e
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PDB id:
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Hydrolase
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Title:
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Crystal structure of recombinant wildtype cdh
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Structure:
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Cyclohexane-1,2-dione hydrolase. Chain: a, b. Engineered: yes
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Source:
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Azoarcus sp. Bh72. Organism_taxid: 62928. Strain: bh72. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.43Å
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R-factor:
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0.123
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R-free:
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0.147
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Authors:
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S.Loschonsky,T.Wacker,S.Waltzer,P.P.Giovannini,M.J.Mcleish, S.L.A.Andrade,M.Mueller
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Key ref:
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S.Loschonsky
et al.
(2014).
Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligation.
Angew Chem Int Ed Engl,
53,
14402-14406.
PubMed id:
DOI:
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Date:
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03-Nov-14
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Release date:
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21-Jan-15
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PROCHECK
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Headers
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References
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P0CH62
(CHDH_AZOSP) -
Cyclohexane-1,2-dione hydrolase from Azoarcus sp
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Seq:
Struc:
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589 a.a.
586 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.7.1.11
- cyclohexane-1,2-dione hydrolase.
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Reaction:
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cyclohexan-1,2-dione + H2O = 6-oxohexanoate + H+
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cyclohexan-1,2-dione
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+
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H2O
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=
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6-oxohexanoate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Angew Chem Int Ed Engl
53:14402-14406
(2014)
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PubMed id:
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Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligation.
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S.Loschonsky,
T.Wacker,
S.Waltzer,
P.P.Giovannini,
M.J.McLeish,
S.L.Andrade,
M.Müller.
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ABSTRACT
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ThDP-dependent cyclohexane-1,2-dione hydrolase (CDH) catalyzes the CC bond
cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, and the asymmetric benzoin
condensation between benzaldehyde and pyruvate. One of the two reactivities of
CDH was selectively knocked down by mutation experiments. CDH-H28A is much less
able to catalyze the CC bond formation, while the ability for CC bond
cleavage is still intact. The double variant CDH-H28A/N484A shows the opposite
behavior and catalyzes the addition of pyruvate to cyclohexane-1,2-dione,
resulting in the formation of a tertiary alcohol. Several acyloins of tertiary
alcohols are formed with 54-94 % enantiomeric excess. In addition to pyruvate,
methyl pyruvate and butane-2,3-dione are alternative donor substrates for CC
bond formation. Thus, the very rare aldehyde-ketone cross-benzoin reaction has
been solved by design of an enzyme variant.
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