Cystathionine gamma-lyase
Name | Cystathionine gamma-lyase |
---|---|
Synonyms | 4.4.1.1 Cysteine-protein sulfhydrase Gamma-cystathionase |
Gene Name | CTH |
Organism | Human |
Amino acid sequence | >lcl|BSEQ0001578|Cystathionine gamma-lyase MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEY SRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRY FRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHG DIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQ NSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQH ELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVL KNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS |
Number of residues | 405 |
Molecular Weight | 44507.64 |
Theoretical pI | 6.69 |
GO Classification |
Functions
carbon-sulfur lyase activity cystathionine gamma-lyase activity homocysteine desulfhydrase activity L-cysteine desulfhydrase activity L-cystine L-cysteine-lyase (deaminating) pyridoxal phosphate binding Processes
cysteine biosynthetic process via cystathionine protein sulfhydration hydrogen sulfide biosynthetic process protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine transsulfuration sulfur amino acid catabolic process cellular nitrogen compound metabolic process cysteine metabolic process small molecule metabolic process positive regulation of I-kappaB kinase/NF-kappaB signaling protein homotetramerization sulfur amino acid metabolic process endoplasmic reticulum unfolded protein response negative regulation of apoptotic signaling pathway cysteine biosynthetic process positive regulation of NF-kappaB transcription factor activity Components
nucleus cytosol extracellular exosome cytoplasm |
General Function | Pyridoxal phosphate binding |
Specific Function | Catalyzes the last step in the trans-sulfuration 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. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function. |
Transmembrane Regions | |
GenBank Protein ID | 262476 |
UniProtKB ID | P32929 |
UniProtKB Entry Name | CGL_HUMAN |
Cellular Location | Cytoplasm |
Gene sequence | >lcl|BSEQ0010559|Cystathionine gamma-lyase (CTH) ATGCAGGAAAAAGACGCCTCCTCACAAGGTTTCCTGCCACACTTCCAACATTTCGCCACG CAGGCGATCCATGTGGGCCAGGATCCAGAGCAATGGACCTCCAGGGCTGTAGTGCCCCCC ATCTCACTGTCCACCACGTTCAAGCAAGGGGCGCCTGGCCAGCACTCGGGTTTTGAATAT AGCCGTTCTGGAAATCCCACTAGGAATTGCCTTGAAAAAGCAGTGGCAGCACTGGATGGG GCTAAGTACTGTACAAACAGGTACTTCAGGCAAGTGGCATCTGAATTTGGATTAAAGATT TCTTTTGTTGATTGTTCCAAAATCAAATTACTAGAGGCAGCAATTACACCAGAAACCAAG CTTGTTTGGATCGAAACCCCCACAAACCCCACCCAGAAGGTGATTGACATTGAAGGCTGT GCACATATTGTCCATAAGCATGGAGACATTATTTTGGTCGTGGATAACACTTTTATGTCA CCATATTTCCAGCGCCCTTTGGCTCTGGGAGCTGATATTTCTATGTATTCTGCAACAAAA TACATGAATGGCCACAGTGATGTTGTAATGGGCCTGGTGTCTGTTAATTGTGAAAGCCTT CATAATAGACTTCGTTTCTTGCAAAACTCTCTTGGAGCAGTTCCATCTCCTATTGATTGT TACCTCTGCAATCGAGGTCTGAAGACTCTACATGTCCGAATGGAAAAGCATTTCAAAAAC GGAATGGCAGTTGCCCAGTTCCTGGAATCTAATCCTTGGGTAGAAAAGGTTATTTATCCT GGGCTGCCCTCTCATCCACAGCATGAGTTGGTGAAGCGTCAGTGTACAGGTTGTACAGGG ATGGTCACCTTTTATATTAAGGGCACTCTTCAGCATGCTGAGATTTTCCTCAAGAACCTA AAGCTATTTACTCTGGCCGAGAGCTTGGGAGGATTCGAAAGCCTTGCTGAGCTTCCGGCA ATCATGACTCATGCATCAGTTCTTAAGAATGACAGAGATGTCCTTGGAATTAGTGACACA CTGATTCGACTTTCTGTGGGCTTAGAGGATGAGGAAGACCTACTGGAAGATCTAGATCAA GCTTTGAAGGCAGCACACCCTCCAAGTGGAAGTCACAGCTAG |
GenBank Gene ID | S52784 |
GeneCard ID | None |
GenAtlas ID | CTH |
HGNC ID | HGNC:2501 |
Chromosome Location | 1 |
Locus | 1p31.1 |
References |
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Related FRC
FRCD ID | Name | Exact Mass | Structure |
---|---|---|---|
L-Cysteine |
121.154 |