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aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme
PLP-dependent transferase
This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor. [1]. 8831789. Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A. Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A;. J Mol Biol 1996;262:202-224. [2]. 9843488. Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolution. Clausen T, Huber R, Prade L, Wahl MC, Messerschmidt A;. EMBO J 1998;17:6827-6838. (from Pfam)
cystathionine gamma-synthase
This family consists of O-succinylhomoserine (thiol)-lyase, one of three different enzymes designated cystathionine gamma-synthase and involved in methionine biosynthesis. In all three cases, sulfur is added by transsulfuration from Cys to yield cystathionine rather than by a sulfhydrylation step that uses H2S directly and bypasses cystathionine.
cystathionine gamma-synthase family protein
cystathionine gamma-synthase family protein which uses use PLP (pyridoxal-5'-phosphate) as a cofactor and may be involved in cysteine or methionine metabolism, similar to Escherichia coli cystathionine gamma-synthase MetB which catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine and L-cysteine, via a gamma-replacement reaction and plays a role in methionine metabolism
Catalyzes the formation of cystathionine from L-cysteine and O-succinyl-L-homoserine
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