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{{enzyme
| Name = cystathionine gamma-synthase
| EC_number = 2.5.1.48
| CAS_number = 9030-70-0
| IUBMB_EC_number = 2/5/1/48
| GO_code = 0003962
| image = 
| width = 
| caption = 
}}
In [[enzymology]], a '''cystathionine gamma-synthase''' ({{EC number|2.5.1.48}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:O<sub>4</sub>-succinyl-L-homoserine + L-cysteine <math>\rightleftharpoons</math> L-cystathionine + succinate

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[O4-succinyl-L-homoserine]] and [[L-cysteine]], whereas its two [[product (chemistry)|products]] are [[L-cystathionine]] and [[succinate]].

This enzyme belongs to the family of [[transferase]]s, specifically those transferring aryl or alkyl groups other than methyl groups.  The systematic name of this enzyme class is '''O4-succinyl-L-homoserine:L-cysteine S-(3-amino-3-carboxypropyl)transferase'''. Other names in common use include '''O-succinyl-L-homoserine succinate-lyase (adding cysteine)''', '''O-succinylhomoserine (thiol)-lyase''', '''homoserine O-transsuccinylase''', '''O-succinylhomoserine synthase''', '''O-succinylhomoserine synthetase''', '''cystathionine synthase''', '''cystathionine synthetase''', '''homoserine transsuccinylase''', '''4-O-succinyl-L-homoserine:L-cysteine''', and '''S-(3-amino-3-carboxypropyl)transferase'''.  This enzyme participates in 4 [[metabolism|metabolic pathways]]: [[methionine metabolism]], [[cysteine metabolism]], [[selenoamino acid metabolism]], and [[sulfur metabolism]].  It employs one [[cofactor (biochemistry)|cofactor]], [[pyridoxal phosphate]].

==References==
{{reflist|1}}
* {{cite journal | author = Flavin M, Slaughter C | year = 1967 | title = Enzymatic synthesis of homocysteine or methionine directly from O-succinyl-homoserine | journal = Biochim. Biophys. Acta.  | volume = 132 | pages = 400&ndash;5  | pmid = 5340123 | issue = 2 }}
* {{cite journal | author = Kaplan MM, Flavin M | year = 1966 | title = Cystathionine gamma-synthetase of Salmonella. Catalytic properties of a new enzyme in bacterial methionine biosynthesis | journal = J. Biol. Chem.  | volume = 241 | pages = 4463&ndash;71  | pmid = 5922970 | issue = 19 }}
* {{cite journal | author = Wiebers JL, Garner HR | year = 1967 | title = Homocysteine and cysteine synthetases of Neurospora crassa Purification, properties, and feedback control of activity | journal = J. Biol. Chem.  | volume = 242 | pages = 12&ndash;23  | pmid = 6016326 | issue = 1 }}
* {{cite journal | author = Wiebers JL, Garner HR | year = 1967 | title = Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast, and Escherichia coli | journal = J. Biol. Chem.  | volume = 242 | pages = 5644&ndash;9  | pmid = 12325384 | issue = 23 }}
* {{cite journal | author = Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A | year = 1998 | title = Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution | journal = EMBO J.  | volume = 17 | pages = 6827&ndash;38  | pmid = 9843488 | doi = 10.1093/emboj/17.23.6827 | issue = 23 | pmc = 1171030 }}
* {{cite journal | author = Ravanel S, Gakiere B, Job D, Douce R | date =  Pt 2 | title = Cystathionine gamma-synthase from Arabidopsis thaliana: purification and biochemical characterization of the recombinant enzyme overexpressed in Escherichia coli | journal = Biochem. J.  | volume = 331 | pages = 639&ndash;48  | pmid = 9531508 | pmc = 1219399 }}

[[Category:EC 2.5.1]]
[[Category:Pyridoxal phosphate enzymes]]
[[Category:Enzymes of unknown structure]]


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