Literature summary extracted from

Sun, Q.; Collins, R.; Huang, S.; Holmberg-Schiavone, L.; Anand, G.S.; Tan, C.H.; van-den-Berg, S.; Deng, L.W.; Moore, P.K.; Karlberg, T.; Sivaraman, J.
Structural basis for the inhibition mechanism of human cystathionine {gamma}-lyase, an enzyme responsible for the production of H2S (2009), J. Biol. Chem., 284, 3076-3085.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
4.4.1.1	expressed in Escherichia coli	Homo sapiens

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.4.1.1	using sitting drop and hanging drop vapor diffusion methods at room temperature	Homo sapiens

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
4.4.1.1	DL-propargylglycine	-	Homo sapiens

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
4.4.1.1	0.5	-	L-cystathionine	-	Homo sapiens
4.4.1.1	2.75	-	L-cysteine	-	Homo sapiens

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.4.1.1	Homo sapiens	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
4.4.1.1	gel filtration	Homo sapiens

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4.4.1.1	L-cystathionine + H2O	-	Homo sapiens	L-cysteine + NH3 + 2-oxobutanoate	-	?
4.4.1.1	L-cysteine + H2O	-	Homo sapiens	sulfide + NH3 + pyruvate	-	?

Subunits

EC Number	Subunits	Comment	Organism
4.4.1.1	oligomer	-	Homo sapiens

Synonyms

EC Number	Synonyms	Comment	Organism
4.4.1.1	CSE	-	Homo sapiens
4.4.1.1	cystathionine gamma-lyase	-	Homo sapiens
4.4.1.1	hCSE	-	Homo sapiens

Turnover Number [1/s]

EC Number	Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
4.4.1.1	0.4	-	L-cysteine	-	Homo sapiens
4.4.1.1	7.5	-	L-cystathionine	-	Homo sapiens

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
4.4.1.1	pyridoxal 5'-phosphate	-	Homo sapiens

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Release 2023.1 (January 2023)