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Literature summary extracted from

  • Jones, A.R.; Rentergent, J.; Scrutton, N.S.; Hay, S.
    Probing reversible chemistry in coenzyme B12 -dependent ethanolamine ammonia lyase with kinetic isotope effects (2015), Chemistry, 21, 8826-8831 .
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.7 Salmonella enterica
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.7 acetaldehyde + NH3 by selectively deuterating the substrate (ethanolamine) and/or the beta-carbon of the 5'-deoxyadenosyl moiety of the intrinsiccoenzyme B12, it is possible to experimentally probe both the forward and reverse hydrogen atom transfers between the 5'-deoxyadenosyl radical and substrate during single turnover stopped-flow measurements Salmonella enterica ethanolamine
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4.3.1.7 ethanolamine by selectively deuterating the substrate (ethanolamine) and/or the beta-carbon of the 5'-deoxyadenosyl moiety of the intrinsic coenzyme B12, it is possible to experimentally probe both the forward and reverse hydrogen atom transfers between the 5'-deoxyadenosyl radical and substrate during single turnover stopped-flow measurements Salmonella enterica acetaldehyde + NH3
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r

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.7 coenzyme B12 dependent on Salmonella enterica