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Structural insight into the molecular mechanism of allosteric activation of human cystathionine beta-synthase by S-adenosylmethionine.
Ereño-Orbea J, Majtan T, Oyenarte I, Kraus JP, Martínez-Cruz LA. Ereño-Orbea J, et al. Proc Natl Acad Sci U S A. 2014 Sep 16;111(37):E3845-52. doi: 10.1073/pnas.1414545111. Epub 2014 Sep 2. Proc Natl Acad Sci U S A. 2014. PMID: 25197074 Free PMC article.
In contrast to CBSs from lower organisms, human CBS (hCBS) is allosterically activated by S-adenosylmethionine (AdoMet), which binds to the regulatory domain and triggers a conformational change that allows the protein to progress from the basal …
In contrast to CBSs from lower organisms, human CBS (hCBS) is allosterically activated by S-adenosylmethionin
Conformational properties of nine purified cystathionine beta-synthase mutants.
Hnízda A, Majtan T, Liu L, Pey AL, Carpenter JF, Kodíček M, Kožich V, Kraus JP. Hnízda A, et al. Biochemistry. 2012 Jun 12;51(23):4755-63. doi: 10.1021/bi300435e. Epub 2012 May 30. Biochemistry. 2012. PMID: 22612060 Free PMC article.
Protein misfolding due to missense mutations is a common pathogenic mechanism in cystathionine beta-synthase (CBS) deficiency. In our previous studies, we successfully expressed, purified, and characterized nine CBS mutant enzymes containing the follow …
Protein misfolding due to missense mutations is a common pathogenic mechanism in cystathionine beta-synthase (CB …
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