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Literature summary for 4.4.1.1 extracted from

  • Kraus, J.P.; Hasek, J.; Kozich, V.; Collard, R.; Venezia, S.; Janosíková, B.; Wang, J.; Stabler, S.P.; Allen, R.; Jakobs, C.; Finn, C.T.; Chien, Y.H.; Hwu, W.L.; Hegele, R.A.; Mudd, S.H.
    Cystathionine gamma-lyase: Clinical, metabolic, genetic, and structural studies (2009), Mol. Genet. Metab., 97, 250-259.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli XL-1 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
R197C the mutant shows about 44% activity compared to the wild type enzyme Homo sapiens
R62H exchange of Arg62 for His62 shifts the geometry of the active site, decreases the strength of pyridoxal 5'-phosphate binding, and makes this bond pH dependent under physiological conditions Homo sapiens
T311I the mutant shows wild type activity Homo sapiens
T67I the mutant shows about 13% activity compared to the wild type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
DL-propargylglycine
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P32929
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer
-
Homo sapiens

Synonyms

Synonyms Comment Organism
CTH
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Homo sapiens

General Information

General Information Comment Organism
malfunction severe loss of cystathionine gamma-lyase activity is accompanied by adverse clinical effects Homo sapiens