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Literature summary for 5.3.3.1 extracted from

  • Wilde, T.C.; Blotny, G.; Pollack, R.M.
    Experimental evidence for enzyme-enhanced coupled motion/quantum mechanical hydrogen tunneling by ketosteroid isomerase (2008), J. Am. Chem. Soc., 130, 6577-6585.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D99A secondary kinetic isotope effects similar to wild-type. Mutation does not significantly decrease the contribution of coupled motion/hydrogen tunneling to the enzymatic reaction Comamonas testosteroni
Y14F secondary kinetic isotope effects similar to wild-type. Mutation does not significantly decrease the contribution of coupled motion/hydrogen tunneling to the enzymatic reaction Comamonas testosteroni

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
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Reaction

Reaction Comment Organism Reaction ID
a 3-oxo-DELTA5-steroid = a 3-oxo-DELTA4-steroid enzyme enhances the coupled motion/hydrogen tunneling contribution to the rate acceleration over the solution reaction Comamonas testosteroni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
androst-5-ene-3,17-dione alpha-secondary deuterium kinetic isotope effects at C6 of the steroid. Presence of coupled motion/hydrogen tunneling in the enzyme-catalyzed reaction Comamonas testosteroni androst-4-ene-3,17-dione
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