Cystathionine beta-lyase

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spinqualitylabelsall models E. coli cystathionine β-lyase complex with PLP derivative and hepes (PDB code 4itg) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Cystathionine β-lyase (CBL) belongs to a family of PLP-dependent enzymes which cleave C β-S bonds in a variety of subtsrates. CBL catalyzes a reaction specific for methionine biosynthesis[1]. CBL converts L-cystathionine to L-homocysteine, pyruvate and ammonia. Structural highlights The structure of the EcCBL shows 3 spatially different domains. The (residues 1-60) contributes to the . The (residues 61-256) binds to the PLP and the (residues 257-395). and mediates the proton transfer between Cα and Sγ[2]. .

3D structures of Cystathionine β-lyase

Updated on 16-June-2021

• Cystathionine beta-lyase

• • 1ibj – CBL + PLP – Arabidopsis thaliana
    
  • 1cl1 – EcCBL + PLP derivative – Escherichia coli
    
  • 4itg – EcCBL (mutant) + PLP derivative
    
  • 1cl2 – EcCBL + aminoethoxy glycine
    
  • 2fq6, 2gqn – EcCBL + inhibitor
    
  • 4itx – EcCBL (mutant) + inhibitor
    
  • 6cja – LpCBL + PLP-Ala + Ser – Legionella pneumophila
    
  • 6cjb – LpCBL + PLP derivative
    
  • 6vju – LpCBL + PLP derivative + PLP
    
  • 6qp3 – CBL + PLP – Bacillus subtilis
    

• Cystathionine gamma-lyase

• • 1qgn – CGL + PLP – tobaco
    
  • 1n8p – CGL + PLP – yeast
    
  • 6ldo – LpCGL (mutant) + L-Ser – Lactobacillus plantarum
    
  • 6le4 – LpCGL (mutant) + cystathionine
    

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References

1. ↑ Ravanel S, Job D, Douce R. Purification and properties of cystathionine beta-lyase from Arabidopsis thaliana overexpressed in Escherichia coli. Biochem J. 1996 Dec 1;320 ( Pt 2):383-92. doi: 10.1042/bj3200383. PMID:8973544 doi:http://dx.doi.org/10.1042/bj3200383
2. ↑ Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A. Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A. J Mol Biol. 1996 Sep 20;262(2):202-24. PMID:8831789 doi:10.1006/jmbi.1996.0508