B6db activities : 2_5_1

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	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	-Bacteria -Archea -Plants -Fungi
Family	2.5.1.48_a (8) 2.5.1.48_b (10)

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	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	2008/03/11 18:40

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