Cystathionine γ-Lyase (human, recombinant)

Transsulfuration and reverse transsulfuration comprise part of the metabolic interconversion of the sulfur-containing amino acids cysteine and methionine.¹ Reverse transsulfuration is catalyzed by the enzymes cystathionine β-synthase (CBS) and cystathionine γ-lyase (CGL) in fungi and mammals.¹ Specifically, CGL catalyzes the conversion of cystathionine to cysteine in a pyridoxal-5'-phosphate-dependant reaction.² At elevated levels, homocysteine is an independent risk factor for cardiovascular diseases and other complex disorders.² The mammalian transsulfuration pathway is one of two major metabolic routes for homocysteine removal. Besides homocysteine removal, transsulfuration contributes significantly to the intracellular cysteine pool.² Cysteine is used for biosynthesis of glutathione, and is also the primary substrate for H₂S biosynthesis. CGL is one of two major enzymes that catalyzes the formation of H₂S from cysteine. ² H₂S generation is a biological gasotransmitter, a neuromodulator, a vasodilator, and plays an important role in inflammation.²

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1. Steegborn, C., Clausen, T., Sondermann, P., et al. Kinetics and inhibition of recombinant human cystathionine γ-lyase. Toward the rational control of transsulfuration. The Journal of Biological Chemisty 274(18), 12675-12684 (1999).

2. Zhu, W., Lin, A., and Banerjee, R. Kinetic properties of polymorphic variants and pathogenic mutants in human cystathionine γ-lyase. Biochemistry 47(23), 6226-6232 (2008).