Activities | Families | Sequences | Fold types | References | Help
B6db activities: 2.5.1.48

2.5.1.48
Description Cystathionine gamma-synthase
Alternative names O-succinylhomoserine (thiol)-lyase;
Homoserine transsuccinylase.;
Cystathionine synthase;
MetB.
Catalyzed reaction O-succinyl-L-homoserine + L-cysteine = cystathionine + succinate.
Cofactor Pyridoxal-phosphate.
Comments -!- Can also use hydrogen sulfide and methanethiol as substrates producing homocysteine and methionine respectively.
-!- In the absence of thiol, can also catalyse beta,gamma-elimination to form 2-oxobutanoate, succinate and ammonia.

The plant enzyme can also use O-phosphohomoserine as a substrate.

Formerly EC 4.2.99.9.

Subfamily 2.5.1.48a includes enzymes from gram-negative bacteria; subfamily b encompasses enzymes from plants (plastidial proteins) and cyanobacteria.
Prosite PROSITE; PDOC00677;
PDB 1I48; 1I43; 1I41; 1CS1; 1QGN;
Organisms -Eubacteria -Archea -Plants -Fungi
 

Family 

 
Links Enzyme (activities) 2.5.1.48
BRENDA (activities) 2.5.1.48
KEGG (pathways) 2.5.1.48
PLPMDB (PLP mutants) 2.5.1.48
 
References
 Sato D, Shiba T, Mizuno S, Kawamura A, Hanada S, Yamada T, Shinozaki M, Yanagitani M, Tamura T, Inagaki K, Harada S (2017) The hyperthermophilic cystathionine γ-synthase from the aerobic crenarchaeon Sulfolobus tokodaii: expression, purification, crystallization and structural insights Acta Crystallogr F Struct Biol Commun 73 152-158. .

 Kong Y, Wu D, Bai H, Han C, Chen J, Chen L, Hu L, Jiang H, Shen X. (2008) Enzymatic characterization and inhibitor discovery of a new cystathionine {gamma}-synthase from Helicobacter pylori J Biochem 143 59-68.

 Steegborn, C.; Messerschmidt, A.; Laber, B.; Streber, W.; Huber, R.; Clausen, T. (1999) The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity J Mol Biol 290 983-96.

 Ravanel, S.; Gakiere, B.; Job, D.; Douce, R. (1998) Cystathionine gamma-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli Biochem J 331 639-48.

 Wahl, M. C.; Huber, R.; Prade, L.; Marinkovic, S.; Messerschmidt, A.; Clausen, T. (1997) Cloning, purification, crystallization, and preliminary X-ray diffraction analysis of cystathionine gamma-synthase from E. coli FEBS Lett 414 492-6.

Articles on 2.5.1.48
 
last changed 2010/01/27 18:06

B6db activities