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Substitution of a conserved catalytic dyad into 2‐ KPCC causes loss of carboxylation activity

Journal Article · · FEBS Letters
 [1];  [1];  [1];  [1];  [1];  [1]
  1. Department of Chemistry and Biochemistry Montana State University Bozeman MT USA
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The characteristic His–Glu catalytic dyad of the disulfide oxidoreductase ( DSOR ) family of enzymes is replaced in 2‐ketopropyl coenzyme M oxidoreductase/carboxylase (2‐ KPCC ) by the residues Phe–His. 2‐ KPCC is the only known carboxylating member of the DSOR family and has replaced this dyad potentially to eliminate proton‐donating groups at a key position in the active site. Substitution of the Phe–His by the canonical residues results in production of higher relative concentrations of acetone versus the natural product acetoacetate. The results indicate that these differences in 2‐ KPCC are key in discriminating between carbon dioxide and protons as attacking electrophiles.

Sponsoring Organization:
USDOE
Grant/Contract Number:
NONE; FG02-04ER15563
OSTI ID:
1401693
Journal Information:
FEBS Letters, Journal Name: FEBS Letters Journal Issue: 17 Vol. 590; ISSN 0014-5793
Publisher:
Wiley Blackwell (John Wiley & Sons)Copyright Statement
Country of Publication:
Netherlands
Language:
English

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