Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cystathionine gamma-lyase (EC 4.4.1.1) (Cysteine-protein sulfhydrase) (Gamma-cystathionase)

 CGL_HUMAN               Reviewed;         405 AA.
P32929; B4E1R2; E9PDV0; Q53FB3; Q53Y79; Q9H4W7; Q9H4W8;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
10-JAN-2003, sequence version 3.
27-SEP-2017, entry version 181.
RecName: Full=Cystathionine gamma-lyase;
EC=4.4.1.1;
AltName: Full=Cysteine-protein sulfhydrase;
AltName: Full=Gamma-cystathionase;
Name=CTH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ILE-403.
TISSUE=Liver;
PubMed=1339280; DOI=10.1016/0006-291X(92)92265-Y;
Lu Y., O'Dowd B.F., Orrego H., Israel Y.;
"Cloning and nucleotide sequence of human liver cDNA encoding for
cystathionine gamma-lyase.";
Biochem. Biophys. Res. Commun. 189:749-758(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
ILE-403.
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-403.
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=10212249; DOI=10.1074/jbc.274.18.12675;
Steegborn C., Clausen T., Sondermann P., Jacob U., Worbs M.,
Marinkovic S., Huber R., Wahl M.C.;
"Kinetics and inhibition of recombinant human cystathionine gamma-
lyase. Toward the rational control of transsulfuration.";
J. Biol. Chem. 274:12675-12684(1999).
[9]
FUNCTION.
PubMed=19261609; DOI=10.1074/jbc.M808026200;
Chiku T., Padovani D., Zhu W., Singh S., Vitvitsky V., Banerjee R.;
"H2S biogenesis by human cystathionine gamma-lyase leads to the novel
sulfur metabolites lanthionine and homolanthionine and is responsive
to the grade of hyperhomocysteinemia.";
J. Biol. Chem. 284:11601-11612(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
FUNCTION AS CYSTEINE-PROTEIN SULFHYDRASE.
PubMed=22169477; DOI=10.1126/scisignal.2002329;
Krishnan N., Fu C., Pappin D.J., Tonks N.K.;
"H2s-induced sulfhydration of the phosphatase PTP1B and its role in
the endoplasmic reticulum stress response.";
Sci. Signal. 4:RA86-RA86(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-402 IN COMPLEXES WITH
PYRODOXAL PHOSPHATE; NITRATE AND PROPARGYLGLYCINE, FUNCTION, SUBUNIT,
ENZYME REGULATION, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=19019829; DOI=10.1074/jbc.M805459200;
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 H(2)S.";
J. Biol. Chem. 284:3076-3085(2009).
[14]
VARIANTS CSTNU ILE-67 AND GLU-240, AND VARIANT ILE-403.
PubMed=12574942; DOI=10.1007/s00439-003-0906-8;
Wang J., Hegele R.A.;
"Genomic basis of cystathioninuria (MIM 219500) revealed by multiple
mutations in cystathionine gamma-lyase (CTH).";
Hum. Genet. 112:404-408(2003).
[15]
CHARACTERIZATION OF VARIANTS CSTNU ILE-67 AND GLU-240, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=18476726; DOI=10.1021/bi800351a;
Zhu W., Lin A., Banerjee R.;
"Kinetic properties of polymorphic variants and pathogenic mutants in
human cystathionine gamma-lyase.";
Biochemistry 47:6226-6232(2008).
-!- 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. {ECO:0000269|PubMed:19019829,
ECO:0000269|PubMed:19261609, ECO:0000269|PubMed:22169477}.
-!- CATALYTIC ACTIVITY: L-cystathionine + H(2)O = L-cysteine + NH(3) +
2-oxobutanoate. {ECO:0000269|PubMed:10212249,
ECO:0000269|PubMed:19019829}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:10212249,
ECO:0000269|PubMed:18476726, ECO:0000269|PubMed:19019829};
-!- ENZYME REGULATION: Inhibited by propargylglycine, trifluoroalanine
and aminoethoxyvinylglycine. {ECO:0000269|PubMed:10212249,
ECO:0000269|PubMed:19019829}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.5 mM for L-cystathionine {ECO:0000269|PubMed:10212249,
ECO:0000269|PubMed:18476726};
KM=5.4 mM for homocysteine {ECO:0000269|PubMed:10212249,
ECO:0000269|PubMed:18476726};
KM=3.5 mM for cysteine {ECO:0000269|PubMed:10212249,
ECO:0000269|PubMed:18476726};
pH dependence:
Optimum pH is 8.2. {ECO:0000269|PubMed:10212249,
ECO:0000269|PubMed:18476726};
-!- 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). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-749763, EBI-749763;
Q96NT3:GUCD1; NbExp=3; IntAct=EBI-749763, EBI-8293751;
Q6P9E2:RECK; NbExp=5; IntAct=EBI-749763, EBI-10253121;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-749763, EBI-741158;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P32929-1; Sequence=Displayed;
Name=2;
IsoId=P32929-2; Sequence=VSP_006306;
Name=3;
IsoId=P32929-3; Sequence=VSP_047274;
-!- DISEASE: Cystathioninuria (CSTNU) [MIM:219500]: Autosomal
recessive phenotype characterized by abnormal accumulation of
plasma cystathionine, leading to increased urinary excretion.
{ECO:0000269|PubMed:12574942, ECO:0000269|PubMed:18476726}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S52784; AAB24700.1; -; mRNA.
EMBL; S52028; AAB24699.1; -; mRNA.
EMBL; BT006882; AAP35528.1; -; mRNA.
EMBL; AK303946; BAG64874.1; -; mRNA.
EMBL; AK223376; BAD97096.1; -; mRNA.
EMBL; AL354872; CAC12901.1; -; Genomic_DNA.
EMBL; AL354872; CAC12902.1; -; Genomic_DNA.
EMBL; CH471059; EAX06450.1; -; Genomic_DNA.
EMBL; BC015807; AAH15807.1; -; mRNA.
CCDS; CCDS53333.1; -. [P32929-3]
CCDS; CCDS650.1; -. [P32929-1]
CCDS; CCDS651.1; -. [P32929-2]
PIR; JC1362; JC1362.
RefSeq; NP_001177392.1; NM_001190463.1. [P32929-3]
RefSeq; NP_001893.2; NM_001902.5. [P32929-1]
RefSeq; NP_714964.2; NM_153742.4. [P32929-2]
UniGene; Hs.19904; -.
PDB; 2NMP; X-ray; 2.60 A; A/B/C/D=1-402.
PDB; 3COG; X-ray; 2.00 A; A/B/C/D=1-402.
PDB; 3ELP; X-ray; 2.40 A; A/B/C/D=1-405.
PDB; 5EIG; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-405.
PDBsum; 2NMP; -.
PDBsum; 3COG; -.
PDBsum; 3ELP; -.
PDBsum; 5EIG; -.
ProteinModelPortal; P32929; -.
SMR; P32929; -.
BioGrid; 107873; 51.
IntAct; P32929; 6.
MINT; MINT-1479767; -.
STRING; 9606.ENSP00000359976; -.
BindingDB; P32929; -.
DrugBank; DB02328; 2-[(3-Hydroxy-2-Methyl-5-Phosphonooxymethyl-Pyridin-4-Ylmethyl)-Imino]-5-Phosphono-Pent-3-Enoic Acid.
DrugBank; DB04217; L-2-amino-3-butynoic acid.
DrugBank; DB00151; L-Cysteine.
DrugBank; DB00114; Pyridoxal Phosphate.
GuidetoPHARMACOLOGY; 1444; -.
iPTMnet; P32929; -.
PhosphoSitePlus; P32929; -.
BioMuta; CTH; -.
DMDM; 27735163; -.
EPD; P32929; -.
MaxQB; P32929; -.
PaxDb; P32929; -.
PeptideAtlas; P32929; -.
PRIDE; P32929; -.
DNASU; 1491; -.
Ensembl; ENST00000346806; ENSP00000311554; ENSG00000116761. [P32929-2]
Ensembl; ENST00000370938; ENSP00000359976; ENSG00000116761. [P32929-1]
Ensembl; ENST00000411986; ENSP00000413407; ENSG00000116761. [P32929-3]
GeneID; 1491; -.
KEGG; hsa:1491; -.
UCSC; uc001dfd.4; human. [P32929-1]
CTD; 1491; -.
DisGeNET; 1491; -.
EuPathDB; HostDB:ENSG00000116761.11; -.
GeneCards; CTH; -.
HGNC; HGNC:2501; CTH.
HPA; HPA021591; -.
HPA; HPA023300; -.
MalaCards; CTH; -.
MIM; 219500; phenotype.
MIM; 607657; gene.
neXtProt; NX_P32929; -.
OpenTargets; ENSG00000116761; -.
Orphanet; 212; Cystathioninuria.
PharmGKB; PA27004; -.
eggNOG; KOG0053; Eukaryota.
eggNOG; COG0626; LUCA.
GeneTree; ENSGT00390000000312; -.
HOGENOM; HOG000246415; -.
HOVERGEN; HBG005322; -.
InParanoid; P32929; -.
KO; K01758; -.
OMA; HPGRMTH; -.
OrthoDB; EOG091G0C7Z; -.
PhylomeDB; P32929; -.
TreeFam; TF300720; -.
BioCyc; MetaCyc:HS04050-MONOMER; -.
BRENDA; 4.4.1.1; 2681.
Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine.
Reactome; R-HSA-1614603; Cysteine formation from homocysteine.
Reactome; R-HSA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
SABIO-RK; P32929; -.
UniPathway; UPA00136; UER00202.
ChiTaRS; CTH; human.
EvolutionaryTrace; P32929; -.
GenomeRNAi; 1491; -.
PRO; PR:P32929; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116761; -.
CleanEx; HS_CTH; -.
Genevisible; P32929; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0016846; F:carbon-sulfur lyase activity; TAS:Reactome.
GO; GO:0004123; F:cystathionine gamma-lyase activity; IDA:UniProtKB.
GO; GO:0003962; F:cystathionine gamma-synthase activity; IBA:GO_Central.
GO; GO:0047982; F:homocysteine desulfhydrase activity; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0080146; F:L-cysteine desulfhydrase activity; TAS:Reactome.
GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IMP:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IBA:GO_Central.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0019344; P:cysteine biosynthetic process; IDA:UniProtKB.
GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IDA:BHF-UCL.
GO; GO:0006534; P:cysteine metabolic process; TAS:ProtInc.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:UniProtKB.
GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IDA:UniProtKB.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:1904831; P:positive regulation of aortic smooth muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
GO; GO:0044524; P:protein sulfhydration; IMP:UniProtKB.
GO; GO:0018272; P:protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine; IDA:UniProtKB.
GO; GO:0000098; P:sulfur amino acid catabolic process; TAS:Reactome.
GO; GO:0019346; P:transsulfuration; IDA:BHF-UCL.
CDD; cd00614; CGS_like; 1.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 1.
InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
PANTHER; PTHR11808; PTHR11808; 1.
Pfam; PF01053; Cys_Met_Meta_PP; 1.
PIRSF; PIRSF001434; CGS; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00868; CYS_MET_METAB_PP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amino-acid biosynthesis;
Calmodulin-binding; Complete proteome; Cysteine biosynthesis;
Cytoplasm; Disease mutation; Lyase; Polymorphism; Pyridoxal phosphate;
Reference proteome.
CHAIN 1 405 Cystathionine gamma-lyase.
/FTId=PRO_0000114749.
BINDING 62 62 Substrate.
BINDING 114 114 Substrate.
BINDING 119 119 Substrate.
BINDING 339 339 Substrate.
MOD_RES 212 212 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
VAR_SEQ 85 116 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047274.
VAR_SEQ 153 196 Missing (in isoform 2).
{ECO:0000303|PubMed:1339280}.
/FTId=VSP_006306.
VARIANT 67 67 T -> I (in CSTNU; reduces catalytic
activity and affinity for pyridoxal
phosphate; dbSNP:rs28941785).
{ECO:0000269|PubMed:12574942,
ECO:0000269|PubMed:18476726}.
/FTId=VAR_015450.
VARIANT 240 240 Q -> E (in CSTNU; strongly reduces
catalytic activity and affinity for
pyridoxal phosphate; dbSNP:rs28941786).
{ECO:0000269|PubMed:12574942,
ECO:0000269|PubMed:18476726}.
/FTId=VAR_015451.
VARIANT 403 403 S -> I (in dbSNP:rs1021737).
{ECO:0000269|PubMed:12574942,
ECO:0000269|PubMed:1339280,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.4}.
/FTId=VAR_015452.
HELIX 18 24 {ECO:0000244|PDB:3COG}.
HELIX 29 31 {ECO:0000244|PDB:3COG}.
STRAND 36 38 {ECO:0000244|PDB:3COG}.
STRAND 45 47 {ECO:0000244|PDB:5EIG}.
TURN 61 63 {ECO:0000244|PDB:3COG}.
HELIX 66 79 {ECO:0000244|PDB:3COG}.
STRAND 82 88 {ECO:0000244|PDB:3COG}.
HELIX 90 98 {ECO:0000244|PDB:3COG}.
STRAND 106 112 {ECO:0000244|PDB:3COG}.
HELIX 115 123 {ECO:0000244|PDB:3COG}.
HELIX 125 128 {ECO:0000244|PDB:3COG}.
STRAND 131 135 {ECO:0000244|PDB:3COG}.
HELIX 140 146 {ECO:0000244|PDB:3COG}.
STRAND 151 159 {ECO:0000244|PDB:3COG}.
TURN 161 163 {ECO:0000244|PDB:3COG}.
HELIX 169 176 {ECO:0000244|PDB:3COG}.
STRAND 178 180 {ECO:0000244|PDB:3COG}.
STRAND 183 187 {ECO:0000244|PDB:3COG}.
TURN 189 191 {ECO:0000244|PDB:3COG}.
TURN 193 195 {ECO:0000244|PDB:3COG}.
TURN 198 202 {ECO:0000244|PDB:3COG}.
STRAND 204 209 {ECO:0000244|PDB:3COG}.
TURN 210 215 {ECO:0000244|PDB:3COG}.
STRAND 223 227 {ECO:0000244|PDB:3COG}.
HELIX 230 243 {ECO:0000244|PDB:3COG}.
HELIX 249 259 {ECO:0000244|PDB:3COG}.
HELIX 262 281 {ECO:0000244|PDB:3COG}.
STRAND 286 290 {ECO:0000244|PDB:3COG}.
HELIX 300 306 {ECO:0000244|PDB:3COG}.
STRAND 312 320 {ECO:0000244|PDB:3COG}.
HELIX 322 331 {ECO:0000244|PDB:3COG}.
STRAND 333 337 {ECO:0000244|PDB:3COG}.
STRAND 342 345 {ECO:0000244|PDB:3COG}.
STRAND 347 349 {ECO:0000244|PDB:3COG}.
TURN 351 358 {ECO:0000244|PDB:3COG}.
HELIX 361 367 {ECO:0000244|PDB:3COG}.
STRAND 373 377 {ECO:0000244|PDB:3COG}.
HELIX 383 397 {ECO:0000244|PDB:3COG}.
SEQUENCE 405 AA; 44508 MW; 003246D7C1D16723 CRC64;
MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY
SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY
FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG
DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ
NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH
ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL
KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS


Related products :

Catalog number Product name Quantity
E1538b ELISA kit Bos taurus,Bovine,CTH,Cystathionine gamma-lyase,Gamma-cystathionase 96T
E1538m ELISA Cth,Cystathionine gamma-lyase,Gamma-cystathionase,Mouse,Mus musculus 96T
E1538m ELISA kit Cth,Cystathionine gamma-lyase,Gamma-cystathionase,Mouse,Mus musculus 96T
U1538m CLIA Cth,Cystathionine gamma-lyase,Gamma-cystathionase,Mouse,Mus musculus 96T
U1538b CLIA Bos taurus,Bovine,CTH,Cystathionine gamma-lyase,Gamma-cystathionase 96T
E1538b ELISA Bos taurus,Bovine,CTH,Cystathionine gamma-lyase,Gamma-cystathionase 96T
E1538p ELISA CTH,Cystathionine gamma-lyase,Gamma-cystathionase,Pig,Sus scrofa 96T
U1538p CLIA CTH,Cystathionine gamma-lyase,Gamma-cystathionase,Pig,Sus scrofa 96T
E1538p ELISA kit CTH,Cystathionine gamma-lyase,Gamma-cystathionase,Pig,Sus scrofa 96T
E1538h ELISA CTH,Cystathionine gamma-lyase,Gamma-cystathionase,Homo sapiens,Human 96T
E1538h ELISA kit CTH,Cystathionine gamma-lyase,Gamma-cystathionase,Homo sapiens,Human 96T
U1538h CLIA CTH,Cystathionine gamma-lyase,Gamma-cystathionase,Homo sapiens,Human 96T
U1538r CLIA Cth,Cystathionine gamma-lyase,Gamma-cystathionase,PRB-RA,Probasin-related antigen,Rat,Rattus norvegicus 96T
E1538r ELISA kit Cth,Cystathionine gamma-lyase,Gamma-cystathionase,PRB-RA,Probasin-related antigen,Rat,Rattus norvegicus 96T
E1538r ELISA Cth,Cystathionine gamma-lyase,Gamma-cystathionase,PRB-RA,Probasin-related antigen,Rat,Rattus norvegicus 96T
CTH-1333H Protein Recombinant Human Cystathionase (cystathionine gamma-lyase), His-tagged 0.5mg
CTH-1333H Protein: Recombinant Human Cystathionase (cystathionine gamma-lyase), His-tagged 0.5mg
E1381024 Cystathionase (Cystathionine gamma-Lyase) (CTH) ELISA Kit 1
CTLA4 CTH Gene cystathionase (cystathionine gamma-lyase)
GWB-D55600 Anti- CTH (cystathionase (cystathionine gamma-lyase)) Antibody
GS-0495a cystathionase (cystathionine gamma-lyase) primary antibody, Host: Rabbit 200ul
CSB-EL006160PI Pig cystathionase (cystathionine gamma-lyase) (CTH) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL006160HU Human cystathionase (cystathionine gamma-lyase) (CTH) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL006160MO Mouse cystathionase (cystathionine gamma-lyase) (CTH) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL006160BO Bovine cystathionase (cystathionine gamma-lyase) (CTH) ELISA kit, Species Bovine, Sample Type serum, plasma 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur