{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P32929","secondaryAccessions":["B4E1R2","E9PDV0","Q53FB3","Q53Y79","Q9H4W7","Q9H4W8"],"uniProtkbId":"CGL_HUMAN","entryAudit":{"firstPublicDate":"1993-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2003-01-10","entryVersion":225,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10212249"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10727430"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18476726"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19019829"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19261609"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19961860"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22169477"}],"value":"Cystathionine gamma-lyase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10212249"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10727430"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18476726"}],"value":"CGL"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19019829"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19261609"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19961860"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"22169477"}],"value":"CSE"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10212249"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10727430"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18476726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19261609"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19961860"}],"value":"4.4.1.1"}]},"alternativeNames":[{"fullName":{"value":"Cysteine desulfhydrase"}},{"fullName":{"value":"Cysteine-protein sulfhydrase"}},{"fullName":{"value":"Gamma-cystathionase"}},{"fullName":{"value":"Homocysteine desulfhydrase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18476726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19261609"}],"value":"4.4.1.2"}]}]},"genes":[{"geneName":{"value":"CTH"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18757"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8VCN5"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10212249"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18476726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19019829"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19261609"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19961860"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22169477"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29254196"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"18476726"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"18476726"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19019829"}],"value":"Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate (PubMed:10212249, PubMed:18476726, PubMed:19261609, PubMed:19961860). Part of the L-cysteine derived from the trans-sulfuration pathway is utilized for biosynthesis of the ubiquitous antioxidant glutathione (PubMed:18476726). Besides its role in the conversion of L-cystathionine into L-cysteine, it utilizes L-cysteine and L-homocysteine as substrates (at much lower rates than L,L-cystathionine) to produce the endogenous gaseous signaling molecule hydrogen sulfide (H2S) (PubMed:10212249, PubMed:19019829, PubMed:19261609, PubMed:19961860). In vitro, it converts two L-cysteine molecules into lanthionine and H2S, also two L-homocysteine molecules to homolanthionine and H2S, which can be particularly relevant under conditions of severe hyperhomocysteinemia (which is a risk factor for cardiovascular disease, diabetes, and Alzheimer's disease) (PubMed:19261609). Lanthionine and homolanthionine are structural homologs of L,L-cystathionine that differ by the absence or presence of an extra methylene group, respectively (PubMed:19261609). 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 (PubMed:22169477). By generating the gasotransmitter H2S, it participates in a number of physiological processes such as vasodilation, bone protection, and inflammation (Probable) (PubMed:29254196). Plays an essential role in myogenesis by contributing to the biogenesis of H2S in skeletal muscle tissue (By similarity). Can also accept homoserine as substrate (By similarity). 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