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B6db activities: 4.4.1.8

4.4.1.8
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 4.4.1.6.
In some organisms, such as Lactococcus lactis, this activity is carried out by an enzyme that also possesses a gamma-lyase activity (EC 4.4.1.1) and that is very similar to cystathionine gamma-lyases in terms of sequence.
Prosite PROSITE; PDOC00677; PROSITE; PDOC00518;
PDB 1IBJ; 1CL2; 1CL1; 1D2F;
Organisms -Bacteria -Plants -Fungi
 

Family 

4.4.1.8_a (18) 4.4.1.8_b (7) 4.4.1.8_c (12) 4.4.1.8_d (3)
 
Links Enzyme (activities) 4.4.1.8
BRENDA (activities) 4.4.1.8
KEGG (pathways) 4.4.1.8
PLPMDB (PLP mutants) 4.4.1.8
 
References
 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.

Articles on 4.4.1.8
 
last changed 2009/07/01 13:08

B6db activities