Full text data of MPST
MPST
(TST2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
3-mercaptopyruvate sulfurtransferase; MST; 2.8.1.2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
3-mercaptopyruvate sulfurtransferase; MST; 2.8.1.2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00165360
IPI00165360 3-mercaptopyruvate sulfurtransferase bone marrow, Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. May have a role in cyanide degradation or in thiosulfate biosynthesis. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00165360 3-mercaptopyruvate sulfurtransferase bone marrow, Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. May have a role in cyanide degradation or in thiosulfate biosynthesis. soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P25325
ID THTM_HUMAN Reviewed; 297 AA.
AC P25325; O75750;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=3-mercaptopyruvate sulfurtransferase;
DE Short=MST;
DE EC=2.8.1.2;
GN Name=MPST; Synonyms=TST2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1953758; DOI=10.1016/S0006-291X(05)81148-9;
RA Pallini R., Guazzi G.C., Cannella C., Cacace M.G.;
RT "Cloning and sequence analysis of the human liver rhodanese:
RT comparison with the bovine and chicken enzymes.";
RL Biochem. Biophys. Res. Commun. 180:887-893(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Muscle, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 89-112 AND 119-133, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
RX PubMed=4973015;
RA Ampola M.G., Efron M.L., Bixby E.M., Meshorer E.;
RT "Mental deficiency and a new aminoaciduria.";
RL Am. J. Dis. Child. 117:66-70(1969).
RN [8]
RP ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
RX PubMed=4690911; DOI=10.1016/0009-8981(73)90480-4;
RA Niederwiesler A., Giliberti P., Baerlocher K.;
RT "beta-Mercaptolactate cysteine disulfiduria in two normal sisters.
RT Isolation and characterization of beta-mercaptolactate cysteine
RT disulfide.";
RL Clin. Chim. Acta 43:405-416(1973).
RN [9]
RP ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
RX PubMed=6945862; DOI=10.1016/0006-2944(81)90035-1;
RA Hannestad U., Martensson J., Sjodahl R., Sorbo B.;
RT "3-mercaptolactate cysteine disulfiduria: biochemical studies on
RT affected and unaffected members of a family.";
RL Biochem. Med. 26:106-114(1981).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 11-289.
RG Structural genomics consortium (SGC);
RT "Human 3-mercaptopyruvate sulfurtransferase.";
RL Submitted (SEP-2010) to the PDB data bank.
CC -!- FUNCTION: Transfer of a sulfur ion to cyanide or to other thiol
CC compounds. Also has weak rhodanese activity. Detoxifies cyanide
CC and is required for thiosulfate biosynthesis. Acts as an
CC antioxidant. In combination with cysteine aminotransferase (CAT),
CC contributes to the catabolism of cysteine and is an important
CC producer of hydrogen sulfide in the brain, retina and vascular
CC endothelial cells. Hydrogen sulfide H(2)S is an important synaptic
CC modulator, signaling molecule, smooth muscle contractor and
CC neuroprotectant. Its production by the 3MST/CAT pathway is
CC regulated by calcium ions (By similarity).
CC -!- CATALYTIC ACTIVITY: 3-mercaptopyruvate + cyanide = pyruvate +
CC thiocyanate.
CC -!- ENZYME REGULATION: By oxidative stress, and thioredoxin. Under
CC oxidative stress conditions, the catalytic cysteine site is
CC converted to a sulfenate which inhibits the MPST enzyme activity.
CC Reduced thioredoxin cleaves an intersubunit disulfide bond to turn
CC on the redox switch and reactivate the enzyme.
CC -!- SUBUNIT: Monomer; active form (By similarity). Homodimer;
CC disulfide-linked, inactive form (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Mitochondrion (By
CC similarity). Cell junction, synapse, synaptosome (By similarity).
CC -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure
CC conformations suggesting a common evolutionary origin. Only the C-
CC terminal rhodanese domain contains the catalytic cysteine residue
CC (By similarity).
CC -!- DISEASE: Note=Aberrant MPST activity is found in a few cases of
CC mercaptolactate-cysteine disulfiduria (MCDU) characterized by the
CC appearance of large quantaties of the sulfur-containing amino
CC acid, beta-mercaptolactate-cysteine disulfide, in the urine
CC (PubMed:4973015, PubMed:4690911 and PubMed:6945862). Some cases
CC have associated mental retardation (PubMed:4973015 and
CC PubMed:6945862).
CC -!- MISCELLANEOUS: Thioredoxin (Trx) or dihydrolipoic acid (DHLA) are
CC required to release hydrogen sulfide from the persulfide
CC intermediate (By similarity).
CC -!- SIMILARITY: Contains 2 rhodanese domains.
CC -!- CAUTION: Was originally (PubMed:1953758) thought to be rhodanese.
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DR EMBL; X59434; CAA42060.1; -; mRNA.
DR EMBL; CR456523; CAG30409.1; -; mRNA.
DR EMBL; BT019636; AAV38442.1; -; mRNA.
DR EMBL; Z73420; CAA97763.1; -; Genomic_DNA.
DR EMBL; BC003508; AAH03508.1; -; mRNA.
DR EMBL; BC016737; AAH16737.1; -; mRNA.
DR EMBL; BC018717; AAH18717.1; -; mRNA.
DR PIR; JH0461; ROHU.
DR RefSeq; NP_001013454.1; NM_001013436.2.
DR RefSeq; NP_001123989.1; NM_001130517.2.
DR RefSeq; NP_066949.2; NM_021126.5.
DR RefSeq; XP_005261667.1; XM_005261610.1.
DR UniGene; Hs.248267; -.
DR PDB; 3OLH; X-ray; 2.50 A; A=11-289.
DR PDB; 4JGT; X-ray; 2.16 A; A/B/C=11-289.
DR PDBsum; 3OLH; -.
DR PDBsum; 4JGT; -.
DR ProteinModelPortal; P25325; -.
DR SMR; P25325; 8-287.
DR DIP; DIP-613N; -.
DR IntAct; P25325; 1.
DR STRING; 9606.ENSP00000380318; -.
DR PhosphoSite; P25325; -.
DR DMDM; 6226903; -.
DR OGP; P25325; -.
DR REPRODUCTION-2DPAGE; IPI00165360; -.
DR PaxDb; P25325; -.
DR PeptideAtlas; P25325; -.
DR PRIDE; P25325; -.
DR DNASU; 4357; -.
DR Ensembl; ENST00000341116; ENSP00000342333; ENSG00000128309.
DR Ensembl; ENST00000397225; ENSP00000380402; ENSG00000128309.
DR Ensembl; ENST00000401419; ENSP00000384812; ENSG00000128309.
DR Ensembl; ENST00000404802; ENSP00000383950; ENSG00000128309.
DR Ensembl; ENST00000429360; ENSP00000411719; ENSG00000128309.
DR GeneID; 4357; -.
DR KEGG; hsa:4357; -.
DR UCSC; uc003aql.4; human.
DR CTD; 4357; -.
DR GeneCards; GC22P037415; -.
DR HGNC; HGNC:7223; MPST.
DR HPA; HPA001240; -.
DR MIM; 249650; phenotype.
DR MIM; 602496; gene.
DR neXtProt; NX_P25325; -.
DR Orphanet; 1035; Encephalopathy due to beta-mercaptolactate-cysteine disulfiduria.
DR PharmGKB; PA30928; -.
DR eggNOG; COG2897; -.
DR HOGENOM; HOG000157237; -.
DR HOVERGEN; HBG002345; -.
DR KO; K01011; -.
DR OrthoDB; EOG72ZCGB; -.
DR PhylomeDB; P25325; -.
DR ChiTaRS; MPST; human.
DR GeneWiki; MPST; -.
DR GenomeRNAi; 4357; -.
DR NextBio; 17143; -.
DR PRO; PR:P25325; -.
DR ArrayExpress; P25325; -.
DR Bgee; P25325; -.
DR CleanEx; HS_MPST; -.
DR Genevestigator; P25325; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0016784; F:3-mercaptopyruvate sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; TAS:ProtInc.
DR GO; GO:0009440; P:cyanate catabolic process; TAS:ProtInc.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; TAS:ProtInc.
DR Gene3D; 3.40.250.10; -; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Mitochondrion;
KW Redox-active center; Reference proteome; Repeat; Synapse; Synaptosome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 297 3-mercaptopyruvate sulfurtransferase.
FT /FTId=PRO_0000139398.
FT DOMAIN 25 144 Rhodanese 1.
FT DOMAIN 174 288 Rhodanese 2.
FT REGION 145 160 Hinge.
FT ACT_SITE 248 248 Cysteine persulfide intermediate (By
FT similarity).
FT BINDING 188 188 Substrate (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 40 40 N6-acetyllysine (By similarity).
FT DISULFID 264 264 Interchain (with C-264); redox-active (By
FT similarity).
FT CONFLICT 46 48 RRE -> TQ (in Ref. 1; CAA42060).
FT HELIX 13 21
FT STRAND 29 33
FT HELIX 39 41
FT HELIX 45 51
FT TURN 62 64
FT STRAND 71 74
FT HELIX 79 88
FT STRAND 96 100
FT HELIX 110 119
FT STRAND 125 128
FT HELIX 131 137
FT HELIX 160 162
FT HELIX 166 175
FT STRAND 178 182
FT HELIX 186 189
FT HELIX 213 216
FT STRAND 219 221
FT HELIX 226 235
FT STRAND 244 247
FT STRAND 249 252
FT HELIX 255 263
FT STRAND 271 274
FT HELIX 275 283
SQ SEQUENCE 297 AA; 33178 MW; 2313CC15A47A42EA CRC64;
MASPQLCRAL VSAQWVAEAL RAPRAGQPLQ LLDASWYLPK LGRDARREFE ERHIPGAAFF
DIDQCSDRTS PYDHMLPGAE HFAEYAGRLG VGAATHVVIY DASDQGLYSA PRVWWMFRAF
GHHAVSLLDG GLRHWLRQNL PLSSGKSQPA PAEFRAQLDP AFIKTYEDIK ENLESRRFQV
VDSRATGRFR GTEPEPRDGI EPGHIPGTVN IPFTDFLSQE GLEKSPEEIR HLFQEKKVDL
SKPLVATCGS GVTACHVALG AYLCGKPDVP IYDGSWVEWY MRARPEDVIS EGRGKTH
//
ID THTM_HUMAN Reviewed; 297 AA.
AC P25325; O75750;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=3-mercaptopyruvate sulfurtransferase;
DE Short=MST;
DE EC=2.8.1.2;
GN Name=MPST; Synonyms=TST2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1953758; DOI=10.1016/S0006-291X(05)81148-9;
RA Pallini R., Guazzi G.C., Cannella C., Cacace M.G.;
RT "Cloning and sequence analysis of the human liver rhodanese:
RT comparison with the bovine and chicken enzymes.";
RL Biochem. Biophys. Res. Commun. 180:887-893(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Muscle, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 89-112 AND 119-133, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
RX PubMed=4973015;
RA Ampola M.G., Efron M.L., Bixby E.M., Meshorer E.;
RT "Mental deficiency and a new aminoaciduria.";
RL Am. J. Dis. Child. 117:66-70(1969).
RN [8]
RP ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
RX PubMed=4690911; DOI=10.1016/0009-8981(73)90480-4;
RA Niederwiesler A., Giliberti P., Baerlocher K.;
RT "beta-Mercaptolactate cysteine disulfiduria in two normal sisters.
RT Isolation and characterization of beta-mercaptolactate cysteine
RT disulfide.";
RL Clin. Chim. Acta 43:405-416(1973).
RN [9]
RP ASSOCIATION WITH MERCAPTOLACTATE CYSTEINE DISULFIDURIA.
RX PubMed=6945862; DOI=10.1016/0006-2944(81)90035-1;
RA Hannestad U., Martensson J., Sjodahl R., Sorbo B.;
RT "3-mercaptolactate cysteine disulfiduria: biochemical studies on
RT affected and unaffected members of a family.";
RL Biochem. Med. 26:106-114(1981).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 11-289.
RG Structural genomics consortium (SGC);
RT "Human 3-mercaptopyruvate sulfurtransferase.";
RL Submitted (SEP-2010) to the PDB data bank.
CC -!- FUNCTION: Transfer of a sulfur ion to cyanide or to other thiol
CC compounds. Also has weak rhodanese activity. Detoxifies cyanide
CC and is required for thiosulfate biosynthesis. Acts as an
CC antioxidant. In combination with cysteine aminotransferase (CAT),
CC contributes to the catabolism of cysteine and is an important
CC producer of hydrogen sulfide in the brain, retina and vascular
CC endothelial cells. Hydrogen sulfide H(2)S is an important synaptic
CC modulator, signaling molecule, smooth muscle contractor and
CC neuroprotectant. Its production by the 3MST/CAT pathway is
CC regulated by calcium ions (By similarity).
CC -!- CATALYTIC ACTIVITY: 3-mercaptopyruvate + cyanide = pyruvate +
CC thiocyanate.
CC -!- ENZYME REGULATION: By oxidative stress, and thioredoxin. Under
CC oxidative stress conditions, the catalytic cysteine site is
CC converted to a sulfenate which inhibits the MPST enzyme activity.
CC Reduced thioredoxin cleaves an intersubunit disulfide bond to turn
CC on the redox switch and reactivate the enzyme.
CC -!- SUBUNIT: Monomer; active form (By similarity). Homodimer;
CC disulfide-linked, inactive form (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Mitochondrion (By
CC similarity). Cell junction, synapse, synaptosome (By similarity).
CC -!- DOMAIN: Contains two rhodanese domains with different primary
CC structures but with near identical secondary structure
CC conformations suggesting a common evolutionary origin. Only the C-
CC terminal rhodanese domain contains the catalytic cysteine residue
CC (By similarity).
CC -!- DISEASE: Note=Aberrant MPST activity is found in a few cases of
CC mercaptolactate-cysteine disulfiduria (MCDU) characterized by the
CC appearance of large quantaties of the sulfur-containing amino
CC acid, beta-mercaptolactate-cysteine disulfide, in the urine
CC (PubMed:4973015, PubMed:4690911 and PubMed:6945862). Some cases
CC have associated mental retardation (PubMed:4973015 and
CC PubMed:6945862).
CC -!- MISCELLANEOUS: Thioredoxin (Trx) or dihydrolipoic acid (DHLA) are
CC required to release hydrogen sulfide from the persulfide
CC intermediate (By similarity).
CC -!- SIMILARITY: Contains 2 rhodanese domains.
CC -!- CAUTION: Was originally (PubMed:1953758) thought to be rhodanese.
CC -----------------------------------------------------------------------
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DR EMBL; X59434; CAA42060.1; -; mRNA.
DR EMBL; CR456523; CAG30409.1; -; mRNA.
DR EMBL; BT019636; AAV38442.1; -; mRNA.
DR EMBL; Z73420; CAA97763.1; -; Genomic_DNA.
DR EMBL; BC003508; AAH03508.1; -; mRNA.
DR EMBL; BC016737; AAH16737.1; -; mRNA.
DR EMBL; BC018717; AAH18717.1; -; mRNA.
DR PIR; JH0461; ROHU.
DR RefSeq; NP_001013454.1; NM_001013436.2.
DR RefSeq; NP_001123989.1; NM_001130517.2.
DR RefSeq; NP_066949.2; NM_021126.5.
DR RefSeq; XP_005261667.1; XM_005261610.1.
DR UniGene; Hs.248267; -.
DR PDB; 3OLH; X-ray; 2.50 A; A=11-289.
DR PDB; 4JGT; X-ray; 2.16 A; A/B/C=11-289.
DR PDBsum; 3OLH; -.
DR PDBsum; 4JGT; -.
DR ProteinModelPortal; P25325; -.
DR SMR; P25325; 8-287.
DR DIP; DIP-613N; -.
DR IntAct; P25325; 1.
DR STRING; 9606.ENSP00000380318; -.
DR PhosphoSite; P25325; -.
DR DMDM; 6226903; -.
DR OGP; P25325; -.
DR REPRODUCTION-2DPAGE; IPI00165360; -.
DR PaxDb; P25325; -.
DR PeptideAtlas; P25325; -.
DR PRIDE; P25325; -.
DR DNASU; 4357; -.
DR Ensembl; ENST00000341116; ENSP00000342333; ENSG00000128309.
DR Ensembl; ENST00000397225; ENSP00000380402; ENSG00000128309.
DR Ensembl; ENST00000401419; ENSP00000384812; ENSG00000128309.
DR Ensembl; ENST00000404802; ENSP00000383950; ENSG00000128309.
DR Ensembl; ENST00000429360; ENSP00000411719; ENSG00000128309.
DR GeneID; 4357; -.
DR KEGG; hsa:4357; -.
DR UCSC; uc003aql.4; human.
DR CTD; 4357; -.
DR GeneCards; GC22P037415; -.
DR HGNC; HGNC:7223; MPST.
DR HPA; HPA001240; -.
DR MIM; 249650; phenotype.
DR MIM; 602496; gene.
DR neXtProt; NX_P25325; -.
DR Orphanet; 1035; Encephalopathy due to beta-mercaptolactate-cysteine disulfiduria.
DR PharmGKB; PA30928; -.
DR eggNOG; COG2897; -.
DR HOGENOM; HOG000157237; -.
DR HOVERGEN; HBG002345; -.
DR KO; K01011; -.
DR OrthoDB; EOG72ZCGB; -.
DR PhylomeDB; P25325; -.
DR ChiTaRS; MPST; human.
DR GeneWiki; MPST; -.
DR GenomeRNAi; 4357; -.
DR NextBio; 17143; -.
DR PRO; PR:P25325; -.
DR ArrayExpress; P25325; -.
DR Bgee; P25325; -.
DR CleanEx; HS_MPST; -.
DR Genevestigator; P25325; -.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR GO; GO:0016784; F:3-mercaptopyruvate sulfurtransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; TAS:ProtInc.
DR GO; GO:0009440; P:cyanate catabolic process; TAS:ProtInc.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; TAS:ProtInc.
DR Gene3D; 3.40.250.10; -; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF52821; SSF52821; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS00683; RHODANESE_2; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell junction; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Mitochondrion;
KW Redox-active center; Reference proteome; Repeat; Synapse; Synaptosome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 297 3-mercaptopyruvate sulfurtransferase.
FT /FTId=PRO_0000139398.
FT DOMAIN 25 144 Rhodanese 1.
FT DOMAIN 174 288 Rhodanese 2.
FT REGION 145 160 Hinge.
FT ACT_SITE 248 248 Cysteine persulfide intermediate (By
FT similarity).
FT BINDING 188 188 Substrate (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 40 40 N6-acetyllysine (By similarity).
FT DISULFID 264 264 Interchain (with C-264); redox-active (By
FT similarity).
FT CONFLICT 46 48 RRE -> TQ (in Ref. 1; CAA42060).
FT HELIX 13 21
FT STRAND 29 33
FT HELIX 39 41
FT HELIX 45 51
FT TURN 62 64
FT STRAND 71 74
FT HELIX 79 88
FT STRAND 96 100
FT HELIX 110 119
FT STRAND 125 128
FT HELIX 131 137
FT HELIX 160 162
FT HELIX 166 175
FT STRAND 178 182
FT HELIX 186 189
FT HELIX 213 216
FT STRAND 219 221
FT HELIX 226 235
FT STRAND 244 247
FT STRAND 249 252
FT HELIX 255 263
FT STRAND 271 274
FT HELIX 275 283
SQ SEQUENCE 297 AA; 33178 MW; 2313CC15A47A42EA CRC64;
MASPQLCRAL VSAQWVAEAL RAPRAGQPLQ LLDASWYLPK LGRDARREFE ERHIPGAAFF
DIDQCSDRTS PYDHMLPGAE HFAEYAGRLG VGAATHVVIY DASDQGLYSA PRVWWMFRAF
GHHAVSLLDG GLRHWLRQNL PLSSGKSQPA PAEFRAQLDP AFIKTYEDIK ENLESRRFQV
VDSRATGRFR GTEPEPRDGI EPGHIPGTVN IPFTDFLSQE GLEKSPEEIR HLFQEKKVDL
SKPLVATCGS GVTACHVALG AYLCGKPDVP IYDGSWVEWY MRARPEDVIS EGRGKTH
//
MIM
249650
*RECORD*
*FIELD* NO
249650
*FIELD* TI
%249650 MERCAPTOLACTATE-CYSTEINE DISULFIDURIA; MCDU
;;DISULFIDURIA, MIXED
*FIELD* TX
read more
CLINICAL FEATURES
Ampola et al. (1969) described a placid, hypokinetic, 45-year-old male,
the product of brother-sister incest, who had a low IQ, grand mal
seizures, flattened nasal bridge, and excessively arched palate. He was
found in the course of screening mentally retarded patients with the
nitroprusside test. He excreted large amounts of a sulfur-containing
amino acid, shown by Crawhall et al. (1969) to be
beta-mercaptolactate-cysteine disulfide. The structure of the disulfide
is indicated by its name: in one-half of the molecule the-NH2 of
cysteine is replaced by-OH. Administration of cysteine, but not of
methionine, increased excretion of the mixed disulfide (Crawhall et al.,
1971).
During a screening for cystinuria in the regular schools, Niederwieser
et al. (1973) found the same material in the urine of 2 mentally normal
sisters, aged 11 and 13 years.
In Sweden, Hannestad et al. (1981) detected MCDU in a mentally retarded
woman. Her red cells were devoid of activity of the enzyme
mercaptopyruvate sulfurtransferase (MPST; 602496). Both parents and 5
other relatives in a pattern consistent with their being heterozygotes
showed intermediate levels of red cell MST. The presumed heterozygotes
also excreted excessive amounts of mercaptolactate and mercaptoacetate
in the urine.
*FIELD* SA
Crawhall (1978)
*FIELD* RF
1. Ampola, M. G.; Efron, M. L.; Bixby, E. M.; Meshorer, E.: Mental
deficiency and a new aminoaciduria. Am. J. Dis. Child. 117: 66-70,
1969.
2. Crawhall, J. C.: Beta-mercaptolactate-cysteine disulfiduria.In:
Stanbury, J. B.; Wyngaarden, J. B.; Fredrickson, D. S.: Metabolic
Basis of Inherited Disease. New York: McGraw-Hill (pub.) (4th
ed.): 1978. Pp. 504-513.
3. Crawhall, J. C.; Bir, K.; Purkiss, P.; Stanbury, J. B.: Sulfur
amino acids as precursor of beta-mercaptolactate cysteine disulfide
in human subjects. Biochem. Med. 5: 109-115, 1971.
4. Crawhall, J. C.; Parker, R.; Sneddon, W.; Young, E. P.: Beta-mercaptolactate-cysteine
disulfide in the urine of a mentally retarded patient. Am. J. Dis.
Child. 117: 71-82, 1969.
5. Hannestad, U.; Martensson, J.; Sjodahl, R.; Sorbo, B.: 3-Mercaptolactate
cysteine disulfiduria: biochemical studies on affected and unaffected
members of a family. Biochem. Med. 26: 106-114, 1981.
6. Niederwieser, A.; Giliberti, P.; Baerlocher, K.: Beta-mercaptolactate-cysteine
disulfiduria in two normal sisters. Isolation and characterization
of beta-mercaptolactate cysteine disulfide. Clin. Chim. Acta 43:
405-416, 1973.
*FIELD* CS
Neuro:
Placid;
Hypokinetic;
Mental retardation;
Grand mal seizures
HEENT:
Flat nasal bridge;
High arched palate
Lab:
Aminoaciduria;
Beta-mercaptolactate-cysteine disulfiduria;
Mercaptopyruvate sulfurtransferase (MST) deficiency;
Excess urinary mercaptolactate;
Excess urinary mercaptoacetate
Inheritance:
Autosomal recessive
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 12/10/2009
joanna: 3/18/2004
davew: 8/19/1994
mimadm: 2/19/1994
supermim: 3/17/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
*RECORD*
*FIELD* NO
249650
*FIELD* TI
%249650 MERCAPTOLACTATE-CYSTEINE DISULFIDURIA; MCDU
;;DISULFIDURIA, MIXED
*FIELD* TX
read more
CLINICAL FEATURES
Ampola et al. (1969) described a placid, hypokinetic, 45-year-old male,
the product of brother-sister incest, who had a low IQ, grand mal
seizures, flattened nasal bridge, and excessively arched palate. He was
found in the course of screening mentally retarded patients with the
nitroprusside test. He excreted large amounts of a sulfur-containing
amino acid, shown by Crawhall et al. (1969) to be
beta-mercaptolactate-cysteine disulfide. The structure of the disulfide
is indicated by its name: in one-half of the molecule the-NH2 of
cysteine is replaced by-OH. Administration of cysteine, but not of
methionine, increased excretion of the mixed disulfide (Crawhall et al.,
1971).
During a screening for cystinuria in the regular schools, Niederwieser
et al. (1973) found the same material in the urine of 2 mentally normal
sisters, aged 11 and 13 years.
In Sweden, Hannestad et al. (1981) detected MCDU in a mentally retarded
woman. Her red cells were devoid of activity of the enzyme
mercaptopyruvate sulfurtransferase (MPST; 602496). Both parents and 5
other relatives in a pattern consistent with their being heterozygotes
showed intermediate levels of red cell MST. The presumed heterozygotes
also excreted excessive amounts of mercaptolactate and mercaptoacetate
in the urine.
*FIELD* SA
Crawhall (1978)
*FIELD* RF
1. Ampola, M. G.; Efron, M. L.; Bixby, E. M.; Meshorer, E.: Mental
deficiency and a new aminoaciduria. Am. J. Dis. Child. 117: 66-70,
1969.
2. Crawhall, J. C.: Beta-mercaptolactate-cysteine disulfiduria.In:
Stanbury, J. B.; Wyngaarden, J. B.; Fredrickson, D. S.: Metabolic
Basis of Inherited Disease. New York: McGraw-Hill (pub.) (4th
ed.): 1978. Pp. 504-513.
3. Crawhall, J. C.; Bir, K.; Purkiss, P.; Stanbury, J. B.: Sulfur
amino acids as precursor of beta-mercaptolactate cysteine disulfide
in human subjects. Biochem. Med. 5: 109-115, 1971.
4. Crawhall, J. C.; Parker, R.; Sneddon, W.; Young, E. P.: Beta-mercaptolactate-cysteine
disulfide in the urine of a mentally retarded patient. Am. J. Dis.
Child. 117: 71-82, 1969.
5. Hannestad, U.; Martensson, J.; Sjodahl, R.; Sorbo, B.: 3-Mercaptolactate
cysteine disulfiduria: biochemical studies on affected and unaffected
members of a family. Biochem. Med. 26: 106-114, 1981.
6. Niederwieser, A.; Giliberti, P.; Baerlocher, K.: Beta-mercaptolactate-cysteine
disulfiduria in two normal sisters. Isolation and characterization
of beta-mercaptolactate cysteine disulfide. Clin. Chim. Acta 43:
405-416, 1973.
*FIELD* CS
Neuro:
Placid;
Hypokinetic;
Mental retardation;
Grand mal seizures
HEENT:
Flat nasal bridge;
High arched palate
Lab:
Aminoaciduria;
Beta-mercaptolactate-cysteine disulfiduria;
Mercaptopyruvate sulfurtransferase (MST) deficiency;
Excess urinary mercaptolactate;
Excess urinary mercaptoacetate
Inheritance:
Autosomal recessive
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 12/10/2009
joanna: 3/18/2004
davew: 8/19/1994
mimadm: 2/19/1994
supermim: 3/17/1992
supermim: 3/20/1990
ddp: 10/26/1989
marie: 3/25/1988
MIM
602496
*RECORD*
*FIELD* NO
602496
*FIELD* TI
*602496 MERCAPTOPYRUVATE SULFURTRANSFERASE; MPST
;;MST
*FIELD* TX
DESCRIPTION
Mercaptopyruvate sulfurtransferase (EC 2.8.1.2) catalyzes the transfer
read moreof a sulfur atom from mercaptopyruvate to sulfur acceptors like cyanides
or thiol compounds. MPST plays a central role in both cysteine
degradation and cyanide detoxification (summary by Billaut-Laden et al.,
2006).
CLONING
By screening a human adult liver cDNA expression library with polyclonal
antibodies against bovine liver rhodanese (180370), Pallini et al.
(1991) isolated a cDNA, which they thought was rhodanese (TST; 180370),
but which was later said by Aita et al. (1997) to encode
mercaptopyruvate sulfurtransferase (MPST). The MPST cDNA identified by
Pallini et al. (1991) encodes a predicted 295-amino acid protein that is
57% identical to bovine rhodanese. Northern blot analysis identified a
1.4-kb MPST transcript in adult liver. Aita et al. (1997) stated that
MPST and rhodanese share 60% amino acid sequence identity.
GENE FUNCTION
By characterizing the rat enzymes, Nagahara et al. (1995) found that
cytosolic Mst is evolutionarily related to mitochondrial rhodanese.
Their active-site regions are similar, with identical catalytic cys246
and arg185 residues, and both catalyze sulfurtransferase reactions.
Point mutation studies showed that the specificities of their reactions
were determined by other active-site residues: arg247 and lys248 in
rhodanese, and gly247 and ser248 in Mst.
GENE STRUCTURE
Nagahara et al. (2004) determined that the MPST gene contains 2 exons.
It has properties of a housekeeping gene, including a promoter region
with prominent GC-rich sequences with many CpG and GpC dinucleotides,
and a GC box rather than a TATA box. MPST has 4 possible transcriptional
start sites. The intron contains a complementary xenobiotic responsive
element. Point mutagenesis and deletion studies revealed a silencer
element localized around -390C and an enhancer element around -377G.
MAPPING
Hartz (2009) mapped the MPST gene to chromosome 22q12.3 based on an
alignment of the MPST sequence (GenBank GENBANK B1597227) with the
genomic sequence (GRCh37). The TST gene also maps to 22q12.3.
*FIELD* RF
1. Aita, N.; Ishii, K.; Akamatsu, Y.; Ogasawara, Y.; Tanabe, S.:
Cloning and expression of human liver rhodanese cDNA. Biochem. Biophys.
Res. Commun. 231: 56-60, 1997.
2. Billaut-Laden, I.; Rat, E.; Allorge, D.; Crunelle-Thibaut, A.;
Cauffiez, C.; Chevalier, D.; Lo-Guidice, J.-M.; Broly, F.: Evidence
for a functional genetic polymorphism of the human mercaptopyruvate
sulfurtransferase (MPST), a cyanide detoxification enzyme. Toxicol.
Lett. 165: 101-111, 2006.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 12/8/2009.
4. Nagahara, N.; Okazaki, T.; Nishino, T.: Cytosolic mercaptopyruvate
sulfurtransferase is evolutionarily related to mitochondrial rhodanese:
striking similarity in active site amino acid sequence and the increase
in the mercaptopyruvate sulfurtransferase activity of rhodanese by
site-directed mutagenesis. J. Biol. Chem. 270: 16230-16235, 1995.
5. Nagahara, N.; Sreeja, V. G.; Li, Q.; Shimizu, T.; Tsuchiya, T.;
Fujii-Kuriyama, Y.: A point mutation in a silencer module reduces
the promoter activity for the human mercaptopyruvate sulfurtransferase. Biochim.
Biophys. Acta 1680: 176-184, 2004.
6. Pallini, R.; Guazzi, G. C.; Cannella, C.; Cacace, M. G.: Cloning
and sequence analysis of the human liver rhodanese: comparison with
the bovine and chicken enzymes. Biochem. Biophys. Res. Commun. 180:
887-893, 1991.
*FIELD* CN
Patricia A. Hartz - updated: 8/9/2010
Marla J. F. O'Neill - updated: 12/10/2009
*FIELD* CD
Rebekah S. Rasooly: 4/6/1998
*FIELD* ED
mgross: 08/09/2010
mgross: 8/9/2010
carol: 8/4/2010
terry: 12/10/2009
carol: 12/8/2009
psherman: 4/15/1998
psherman: 4/6/1998
*RECORD*
*FIELD* NO
602496
*FIELD* TI
*602496 MERCAPTOPYRUVATE SULFURTRANSFERASE; MPST
;;MST
*FIELD* TX
DESCRIPTION
Mercaptopyruvate sulfurtransferase (EC 2.8.1.2) catalyzes the transfer
read moreof a sulfur atom from mercaptopyruvate to sulfur acceptors like cyanides
or thiol compounds. MPST plays a central role in both cysteine
degradation and cyanide detoxification (summary by Billaut-Laden et al.,
2006).
CLONING
By screening a human adult liver cDNA expression library with polyclonal
antibodies against bovine liver rhodanese (180370), Pallini et al.
(1991) isolated a cDNA, which they thought was rhodanese (TST; 180370),
but which was later said by Aita et al. (1997) to encode
mercaptopyruvate sulfurtransferase (MPST). The MPST cDNA identified by
Pallini et al. (1991) encodes a predicted 295-amino acid protein that is
57% identical to bovine rhodanese. Northern blot analysis identified a
1.4-kb MPST transcript in adult liver. Aita et al. (1997) stated that
MPST and rhodanese share 60% amino acid sequence identity.
GENE FUNCTION
By characterizing the rat enzymes, Nagahara et al. (1995) found that
cytosolic Mst is evolutionarily related to mitochondrial rhodanese.
Their active-site regions are similar, with identical catalytic cys246
and arg185 residues, and both catalyze sulfurtransferase reactions.
Point mutation studies showed that the specificities of their reactions
were determined by other active-site residues: arg247 and lys248 in
rhodanese, and gly247 and ser248 in Mst.
GENE STRUCTURE
Nagahara et al. (2004) determined that the MPST gene contains 2 exons.
It has properties of a housekeeping gene, including a promoter region
with prominent GC-rich sequences with many CpG and GpC dinucleotides,
and a GC box rather than a TATA box. MPST has 4 possible transcriptional
start sites. The intron contains a complementary xenobiotic responsive
element. Point mutagenesis and deletion studies revealed a silencer
element localized around -390C and an enhancer element around -377G.
MAPPING
Hartz (2009) mapped the MPST gene to chromosome 22q12.3 based on an
alignment of the MPST sequence (GenBank GENBANK B1597227) with the
genomic sequence (GRCh37). The TST gene also maps to 22q12.3.
*FIELD* RF
1. Aita, N.; Ishii, K.; Akamatsu, Y.; Ogasawara, Y.; Tanabe, S.:
Cloning and expression of human liver rhodanese cDNA. Biochem. Biophys.
Res. Commun. 231: 56-60, 1997.
2. Billaut-Laden, I.; Rat, E.; Allorge, D.; Crunelle-Thibaut, A.;
Cauffiez, C.; Chevalier, D.; Lo-Guidice, J.-M.; Broly, F.: Evidence
for a functional genetic polymorphism of the human mercaptopyruvate
sulfurtransferase (MPST), a cyanide detoxification enzyme. Toxicol.
Lett. 165: 101-111, 2006.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 12/8/2009.
4. Nagahara, N.; Okazaki, T.; Nishino, T.: Cytosolic mercaptopyruvate
sulfurtransferase is evolutionarily related to mitochondrial rhodanese:
striking similarity in active site amino acid sequence and the increase
in the mercaptopyruvate sulfurtransferase activity of rhodanese by
site-directed mutagenesis. J. Biol. Chem. 270: 16230-16235, 1995.
5. Nagahara, N.; Sreeja, V. G.; Li, Q.; Shimizu, T.; Tsuchiya, T.;
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*FIELD* CN
Patricia A. Hartz - updated: 8/9/2010
Marla J. F. O'Neill - updated: 12/10/2009
*FIELD* CD
Rebekah S. Rasooly: 4/6/1998
*FIELD* ED
mgross: 08/09/2010
mgross: 8/9/2010
carol: 8/4/2010
terry: 12/10/2009
carol: 12/8/2009
psherman: 4/15/1998
psherman: 4/6/1998