Cystathionine beta-lyase
From Proteopedia
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== Function == | == Function == | ||
| - | '''Cystathionine β-lyase''' (CBL) belongs to a family of PLP-dependent enzymes which cleave C β-S bonds in a variety of subtsrates. PLP is a pyridoxal phosphate. CBL catalyzes a reaction specific for methionine biosynthesis<ref>PMID:8973544</ref>. CBL converts L-cystathionine to L-homocysteine, pyruvate and ammonia. '''Cystathionine γ-lyase''' (CGL) is PLP-dependent and breaks cystathionine to cysteine, ketobutyrate and ammonia<ref>PMID:7287665</ref>. | + | '''Cystathionine β-lyase''' (CBL) belongs to a family of PLP-dependent enzymes which cleave C β-S bonds in a variety of subtsrates. PLP is a pyridoxal phosphate. CBL catalyzes a reaction specific for methionine biosynthesis<ref>PMID:8973544</ref>. CBL converts L-cystathionine to L-homocysteine, pyruvate and ammonia. |
| + | *'''Cystathionine γ-lyase''' (CGL) is PLP-dependent and breaks cystathionine to cysteine, ketobutyrate and ammonia<ref>PMID:7287665</ref>. | ||
== Disease == | == Disease == | ||
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**[[6vju]] – LpCBL + PLP derivative + PLP<br /> | **[[6vju]] – LpCBL + PLP derivative + PLP<br /> | ||
**[[6qp3]] – CBL + PLP – ''Bacillus subtilis''<br /> | **[[6qp3]] – CBL + PLP – ''Bacillus subtilis''<br /> | ||
| - | **[[8duy]] – | + | **[[8duy]] – KpCBL – ''Klebsiella pneumoniae''<br /> |
| + | **[[8u99]] – KpCBL (mutant) + PLP + Ser<br /> | ||
| + | **[[8sa7]], [[8sa8]] , [[8saa]], [[8sac]], [[8sae]] – KaCBL (mutant) + PLP – ''Klebsiella aerogenes''<br /> | ||
| + | **[[8sa9]] – KaCBL (mutant) + PLP + oxamate <br /> | ||
| + | **[[8sad]] – KaCBL (mutant) + PLP + malonate <br /> | ||
| + | **[[8sab]], [[8u98]] – KaCBL (mutant) + PLP + amino acid<br /> | ||
| + | **[[8juj]] – BcCBL + PLP – ''Bacillus cereus''<br /> | ||
| + | **[[8jui]] – BcCBL + PLP derivative<br /> | ||
*Cystathionine gamma-lyase | *Cystathionine gamma-lyase | ||
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**[[6ldo]] – LpCGL (mutant) + L-Ser – ''Lactobacillus plantarum''<br /> | **[[6ldo]] – LpCGL (mutant) + L-Ser – ''Lactobacillus plantarum''<br /> | ||
**[[6le4]] – LpCGL (mutant) + cystathionine<br /> | **[[6le4]] – LpCGL (mutant) + cystathionine<br /> | ||
| + | **[[8biu]], [[8bix]] – TgCGL + PLP + cystathionine – ''Toxoplasma gondii''<br /> | ||
| + | **[[8biv]] – TgCGL (mutant) + PLP <br /> | ||
| + | **[[8bis]], [[8biz]] – TgCGL + PLP + amino acid<br /> | ||
| + | **[[8biw]] – TgCGL (mutant) + PLP + amino acid<br /> | ||
*Bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase | *Bifunctional cystathionine gamma-lyase/homocysteine desulfhydrase | ||
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**[[7mct]], [[7mcu]], [[7mcy]] – BCGL + inhibitor + PLP <br /> | **[[7mct]], [[7mcu]], [[7mcy]] – BCGL + inhibitor + PLP <br /> | ||
**[[7mdb]] – BCGL (mutant) + inhibitor + PLP <br /> | **[[7mdb]] – BCGL (mutant) + inhibitor + PLP <br /> | ||
| - | **[[7d7o]] – | + | **[[7d7o]] – BcBCBL + PLP <br /> |
}} | }} | ||
Current revision
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3D structures of Cystathionine β-lyase
Updated on 20-February-2025
References
- ↑ 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
- ↑ Yamanishi T, Tuboi S. The mechanism of the L-cystine cleavage reaction catalyzed by rat liver gamma-cystathionase. J Biochem. 1981 Jun;89(6):1913-21. doi: 10.1093/oxfordjournals.jbchem.a133393. PMID:7287665 doi:http://dx.doi.org/10.1093/oxfordjournals.jbchem.a133393
- ↑ Paul BD, Sbodio JI, Xu R, Vandiver MS, Cha JY, Snowman AM, Snyder SH. Cystathionine gamma-lyase deficiency mediates neurodegeneration in Huntington's disease. Nature. 2014 May 1;509(7498):96-100. doi: 10.1038/nature13136. Epub 2014 Mar 26. PMID:24670645 doi:http://dx.doi.org/10.1038/nature13136
- ↑ 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
