Selenocysteine lyase

From Proteopedia

Function Selenocysteine lyase (SCL), (CsbD) or cysteine desulferase catalyzes the breakdown of Selenocysteine to alanine and H2Se. SCL uses PLP as a coenzyme[1]. Selenocysteine is a naturally occuring analog of cysteine in which the sulfur atom is substituted by selenium. This seleno-amino acid is a component of selenoproteins and is incorporated into them by a special tRNA with anticodon complimentary to UGA codon[2]. Relevance Knockout SCL mice show effects on their hepatic glucose and lipid homeostasis[3]. Structural highlights Rat SCL structure shows the PLP moiety and bound L-cysteine within the active site cavity. The cysteine carboxyl end forms salt bridge with SCL Arg and 2 hydrogen bonds with Ser and Asn while its amino group forms 2 hydrogen bonds with Ser and Ala[4]. Water molecules are shown as red spheres. PLP interactions. Whole active site.

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3D structures of selenocysteine lyase

Updated on 15-November-2023

3gzc, 3gzd - hSCL + PLP derivative - human
3a9x - rSCL + PLP - rat
3a9z - rSCL + PLP + selenopropionate
3a9y - rSCL + PLP + cysteine
4q75 - AtSCL + PLP derivative + cysteine derivative - Arabidopsis thaliana
4q76 - AtSCL (mutant) + PLP derivative + cysteine derivative
1jf9, 1c0n, 6ndn, 6o10, 7rrn, 7ruj, 7rw3 - EcCsdB + PLP - Escherichia coli
6o12 - EcCsdB (mutant) + PLP
1kmj, 1kmk, 5db5, 6mr2, 6uy5 - EcCsdB + PLP + cysteine derivative
6mr6, 6mre, 6mrh, 6mri, 6o13 - EcCsdB (mutant) + PLP + cysteine derivative
6o11 - EcCsdB (mutant) + cysteine derivative
5ft4, 5ft5, 5ft6 - EcCsdA + PLP
1i29 - EcCsdB + PLP + propagylglycine
5ft8 - EcCsdA + CsdE + PLP
7tlm - ApSCL + PLP + Ala – Atopobium parvulum
7tlq, 7tlr - ApSCL (mutant) + PLP

References

1. ↑ Esaki N, Nakamura T, Tanaka H, Soda K. Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme. J Biol Chem. 1982 Apr 25;257(8):4386-91. PMID:6461656
2. ↑ Stadtman TC. Selenocysteine Lyase. EcoSal Plus. 2004 Dec;1(1). doi: 10.1128/ecosalplus.3.6.1.1.1. PMID:26443359 doi:http://dx.doi.org/10.1128/ecosalplus.3.6.1.1.1
3. ↑ Seale LA, Hashimoto AC, Kurokawa S, Gilman CL, Seyedali A, Bellinger FP, Raman AV, Berry MJ. Disruption of the selenocysteine lyase-mediated selenium recycling pathway leads to metabolic syndrome in mice. Mol Cell Biol. 2012 Oct;32(20):4141-54. doi: 10.1128/MCB.00293-12. Epub 2012 Aug , 13. PMID:22890841 doi:http://dx.doi.org/10.1128/MCB.00293-12
4. ↑ Omi R, Kurokawa S, Mihara H, Hayashi H, Goto M, Miyahara I, Kurihara T, Hirotsu K, Esaki N. Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase. J Biol Chem. 2010 Apr 16;285(16):12133-9. Epub 2010 Feb 17. PMID:20164179 doi:10.1074/jbc.M109.084475