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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
Cystathionine gamma-lyase
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| http://www.biopax.org/relea... |
CGL_HUMAN
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| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
4.4.1.1,
Gamma-cystathionase
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| http://www.biopax.org/relea... |
FUNCTION: Catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. CATALYTIC ACTIVITY: L-cystathionine + H(2)O = L-cysteine + NH(3) + 2-oxobutanoate. COFACTOR: Pyridoxal phosphate. ENZYME REGULATION: Inhibited by propargylglycine, trifluoroalanine and aminoethoxyvinylglycine. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 mM for L-cystathionine; KM=5.4 mM for homocysteine; KM=3.5 mM for cysteine; pH dependence: Optimum pH is 8.2; PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L- cysteine from L-homocysteine and L-serine: step 2/2. SUBUNIT: Homotetramer. Interacts with CALM in a calcium-dependent manner (By similarity). SUBCELLULAR LOCATION: Cytoplasm. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P32929-1; Sequence=Displayed; Name=2; IsoId=P32929-2; Sequence=VSP_006306; PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. DISEASE: Defects in CTH are the cause of cystathioninuria (CSTNU) [MIM:219500]. It is an autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine, leading to increased urinary excretion. SIMILARITY: Belongs to the trans-sulfuration enzymes family. WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/CTH"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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