Cystathionine beta-synthase
FunctionCystathionine β-synthase (CBS) catalyzes the PLP-dependent interconversion of cysteine and homocysteine. In bacterial systems CBS catalyzes the transfer of thiol from cysteine to homocysteine and in mammalian systems from homocysteine to cysteine[1].. DiseaseCBS deficiency causes homocysteinuria which affects the eye, skeletal system, vascular system and the CNS[2]. Mutations in Ala114, Ile278, G305 and G307 were found to be involved in homocysteinuria[3]. Structural highlightsThe structure of the complex of CBS with heme, PLP and SAM shows the N-terminal domain which binds the heme cofactor interacting with Cys52 and His65. The catalytic core interacts with the PLP cofactor at Lys119 and a C-terminal regulatory domain. 3D structures of cystathionine β-synthaseCystathionine β-synthase 3D structures
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ReferencesReferences
- ↑ Zuhra K, Augsburger F, Majtan T, Szabo C. Cystathionine-beta-Synthase: Molecular Regulation and Pharmacological Inhibition. Biomolecules. 2020 Apr 30;10(5). pii: biom10050697. doi: 10.3390/biom10050697. PMID:32365821 doi:http://dx.doi.org/10.3390/biom10050697
- ↑ Picker JD, Levy HL. Homocystinuria Caused by Cystathionine Beta-Synthase Deficiency PMID:20301697
- ↑ Miles EW, Kraus JP. Cystathionine beta-synthase: structure, function, regulation, and location of homocystinuria-causing mutations. J Biol Chem. 2004 Jul 16;279(29):29871-4. Epub 2004 Apr 15. PMID:15087459 doi:http://dx.doi.org/10.1074/jbc.R400005200