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Literature summary for 4.2.1.22 extracted from

  • Niu, W.; Wang, J.; Qian, J.; Wang, M.; Wu, P.; Chen, F.; Yan, S.
    Allosteric control of human cystathionine beta-synthase activity by a redox active disulfide bond (2018), J. Biol. Chem., 293, 2523-2533 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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General Information

General Information Comment Organism
physiological function the central domain of CBS contains a 272CXXC275 motif which exists in oxidized and reduced states. The activity of reduced CBS is 2-3fold greater than that of the oxidized enzyme, and substitution of either cysteine in CXXC motif leads to a loss of redox sensitivity. The Cys272-Cys275 disulfide bond in CBS has a midpoint potential of -314 mV at pH 7.4. Stressing HEK-293 cells with dithiothreitol results in more reduced enzyme and a concomitant increase in H2S production in live HEK293 cells Homo sapiens