Cystathionine beta-lyase

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Current revision (09:00, 20 February 2025) (edit) (undo)
 
Line 31: Line 31:
**[[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]] – CBL – ''Klebsiella pneumoniae''<br />
+
**[[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
Line 39: Line 46:
**[[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
Line 49: Line 60:
**[[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]] – BCBL + PLP – ''Bacillus cereus''<br />
+
**[[7d7o]] – BcBCBL + PLP <br />
}}
}}

Current revision

E. coli cystathionine β-lyase complex with PLP derivative and hepes (PDB code 4itg)

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3D structures of Cystathionine β-lyase

Updated on 20-February-2025

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. 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
  3. 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
  4. 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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