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Literature summary for 4.3.1.7 extracted from

  • Zhu, C.; Warncke, K.
    Kinetic isolation and characterization of the radical rearrangement step in coenzyme B12-dependent ethanolamine ammonia-lyase (2010), J. Am. Chem. Soc., 132, 9610-9615.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information the transient decay reaction kinetics of the 1,1,2,2-2H4-aminoethanol generated CoII-substrate radical pair catalytic intermediate involve sequential passage through the rearrangement step substrate radical to product radical, and the step product radical to diamagnetic product involves hydrogen atom transfer from carbon C5' of the adenosine moiety of the cofactor to the product radical C2 center. The decay kinetics for the 2H-substrate radical over 190-207 K represent two non-interacting populations. The fast observed rate constant kobs represents the rate constant for the radical rearrangement, and this step is the rate determining step in substrate radical decay Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
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