4d5g: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CHDH_AZOSP CHDH_AZOSP]] Catalyzes the ring-opening cleavage of the alicyclic alcohol cyclohexane-1,2-dione.[REFERENCE:1] | [[http://www.uniprot.org/uniprot/CHDH_AZOSP CHDH_AZOSP]] Catalyzes the ring-opening cleavage of the alicyclic alcohol cyclohexane-1,2-dione.[REFERENCE:1] | ||
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== Publication Abstract from PubMed == | |||
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. | |||
Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligation.,Loschonsky S, Wacker T, Waltzer S, Giovannini PP, McLeish MJ, Andrade SL, Muller M Angew Chem Int Ed Engl. 2014 Dec 22;53(52):14402-6. doi: 10.1002/anie.201408287. , Epub 2014 Nov 7. PMID:25382418<ref>PMID:25382418</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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</StructureSection> | </StructureSection> | ||