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B6db activities:
Description Cystathionine beta-lyase
Alternative names Beta-cystathionase;
Beta C-S lyase;
Cysteine lyase;
Cystine lyase.
Catalyzed reaction Cystathionine + H(2)O = L-homocysteine + NH(3) + pyruvate.
Cofactor Pyridoxal-phosphate.
Comments -!- The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds.
-!- Possibly identical, in yeast, with EC
In some organisms, such as Lactococcus lactis, this activity is carried out by an enzyme that also possesses a gamma-lyase activity (EC and that is very similar to cystathionine gamma-lyases in terms of sequence.
Prosite PROSITE; PDOC00677; PROSITE; PDOC00518;
PDB 1IBJ; 1CL2; 1CL1; 1D2F;
Organisms -Eubacteria -Plants -Fungi

Family (0) (0) (0) (0)
Links Enzyme (activities)
BRENDA (activities)
KEGG (pathways)
PLPMDB (PLP mutants)
 Oogai S, Fukuta M, Watanabe K, Inafuku M, Oku H (2019) Molecular characterization of mimosinase and cystathionine β-lyase in the Mimosoideae subfamily member Mimosa pudica J Plant Res 132 667-680.

 Kato S, Oikawa T (2018) A Novel Bifunctional Amino Acid Racemase With Multiple Substrate Specificity, MalY From Lactobacillus sakei LT-13: Genome-Based Identification and Enzymological Characterization Front Microbiol 7 403.

 Holt S, Cordente AG, Williams SJ, Capone DL, Jitjaroen W, Menz IR, Curtin C, Anderson PA. (2011) Engineering Saccharomyces cerevisiae to release 3-Mercaptohexan-1-ol during fermentation through overexpression of an S. cerevisiae Gene, STR3, for improvement of wine aroma Appl Environ Microbiol 77 3626-32.

 Gidijala L, van der Klei IJ, Veenhuis M, Kiel JA. (2007) Reprogramming Hansenula polymorpha for penicillin production: expression of the Penicillium chrysogenum pcl gene FEMS Yeast Res 7 1160-7.

 Arai R, Nishimoto M, Toyama M, Terada T, Kuramitsu S, Shirouzu M, Yokoyama S. (2005) Conserved protein TTHA1554 from Thermus thermophilus HB8 binds to glutamine synthetase and cystathionine beta-lyase Biochim Biophys Acta 1750 40-7.

 Breitinger, U.; Clausen, T.; Ehlert, S.; Huber, R.; Laber, B.; Schmidt, F.; Pohl, E.; Messerschmidt, A. (2001) The three-dimensional structure of cystathionine beta-lyase from Arabidopsis and its substrate specificity Plant Physiol 126 631-42.

 Clausen, T.; Schlegel, A.; Peist, R.; Schneider, E.; Steegborn, C.; Chang, Y,S.; Haase, Av Bourenkov, G.P.; Bartunik, H.D.; Boos, W. (2000) X-ray structure of MalY from Escherichia coli: a pyridoxal 5'-phosphate-dependent enzyme acting as a modulator in mal gene expression EMBO J 19 831-42.

 Sienko, M.; Paszewski, A. (1999) The metG gene of Aspergillus nidulans encoding cystathionine beta-lyase: cloning and analysis Curr Genet 35 638-46.

 Laber, B.; Clausen, T.; Huber, R.; Messerschmidt, A.; Egner, U.; Muller-Fahrnow, A.; Pohlenz, H. D. (1996) Cloning, purification, and crystallization of Escherichia coli cystathionine beta-lyase FEBS Lett 379 94-6.

 Ravanel, S.; Job, D.; Douce, R. (1996) Purification and properties of cystathionine beta-lyase from Arabidopsis thaliana overexpressed in Escherichia coli Biochem J 320 383-92.

 Zdych E. Peist, R. Reidl, J. Boos, W. (1995) MalY of Escherichia coli is an enzyme with the activity of a beta C-S lyase (cystathionase) J. Bacteriol. 177 5035-5039.

 Gentry-Weeks, C. R.; Keith, J. M.; Thompson, J. (1993) Toxicity of Bordetella avium beta-cystathionase toward MC3T3-E1 osteogenic cells J Biol Chem 268 7298-314.

 Park, Y. M.; Stauffer, G. V. (1987) Cloning and characterization of the metC gene from Salmonella typhimurium LT2 Gene 60 291-7.

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last changed 2019/06/20 13:23

B6db activities