UniProt:P25325 MPST

chain
  • initiator methionine:1
  • chain:2-297
checksum 2313CC15A47A42EA
comment
  • FUNCTION Transfer of a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity. Detoxifies cyanide and is required for thiosulfate biosynthesis. Acts as an antioxidant. In combination with cysteine aminotransferase (CAT), contributes to the catabolism of cysteine and is an important producer of hydrogen sulfide in the brain, retina and vascular endothelial cells. Hydrogen sulfide H(2)S is an important synaptic modulator, signaling molecule, smooth muscle contractor and neuroprotectant. Its production by the 3MST/CAT pathway is regulated by calcium ions.CATALYTIC ACTIVITY 2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol = [thioredoxin]-disulfide + hydrogen sulfide + pyruvate + H(+)ACTIVITY REGULATION By oxidative stress, and thioredoxin. Under oxidative stress conditions, the catalytic cysteine site is converted to a sulfenate which inhibits the MPST enzyme activity. Reduced thioredoxin cleaves an intersubunit disulfide bond to turn on the redox switch and reactivate the enzyme.SUBUNIT Monomer (active form). Homodimer; disulfide-linked (inactive form).INTERACTION Contains two rhodanese domains with different primary structures but with near identical secondary structure conformations suggesting a common evolutionary origin. Only the C-terminal rhodanese domain contains the catalytic cysteine residue (By similarity).DISEASE Aberrant MPST activity is found in a few cases of mercaptolactate-cysteine disulfiduria (MCDU) characterized by the appearance of large quantaties of the sulfur-containing amino acid, beta-mercaptolactate-cysteine disulfide, in the urine (PubMed:4690911, PubMed:4973015, PubMed:6945862). Some cases have associated intellectual disability (PubMed:4973015, PubMed:6945862).MISCELLANEOUS Thioredoxin (Trx) or dihydrolipoic acid (DHLA) are required to release hydrogen sulfide from the persulfide intermediate.CAUTION Was originally thought to be rhodanese.SEQUENCE CAUTION Truncated N-terminus.SEQUENCE CAUTION Truncated N-terminus.
crossReference
databaseName UniProt
dbId 66011
description
  • recommendedName: 3-mercaptopyruvate sulfurtransferase shortName: MST ecNumber evidence="2"2.8.1.2
displayName UniProt:P25325 MPST
geneName
  • MPST
  • TST2
identifier P25325
isSequenceChanged false
keyword
  • 3D-structure
  • Acetylation
  • Alternative splicing
  • Cytoplasm
  • Direct protein sequencing
  • Disulfide bond
  • Mitochondrion
  • Phosphoprotein
  • Proteomics identification
  • Redox-active center
  • Reference proteome
  • Repeat
  • Synapse
  • Synaptosome
  • Transferase
modified [InstanceEdit:9963647] Weiser, Joel, 2025-08-15
moleculeType Protein
name
  • MPST
otherIdentifier
  • 11753895_x_at
  • 16929707
  • 203524_PM_s_at
  • 203524_s_at
  • 36124_at
  • 3944621
  • 3944622
  • 3944623
  • 3944625
  • 3944626
  • 3944627
  • 3944628
  • 3944629
  • 3944630
  • 3944631
  • 3944632
  • 3944634
  • 4357
  • 8072777
  • A_14_P126525
  • A_23_P132285
  • GE60432
  • GO:0000098
  • GO:0001822
  • GO:0001889
  • GO:0004792
  • GO:0005515
  • GO:0005737
  • GO:0005739
  • GO:0005759
  • GO:0006520
  • GO:0006790
  • GO:0009440
  • GO:0009636
  • GO:0016740
  • GO:0016783
  • GO:0016784
  • GO:0019346
  • GO:0021510
  • GO:0042802
  • GO:0043005
  • GO:0045202
  • GO:0048856
  • GO:0070062
  • GO:0070814
  • HMNXSV003010928
  • HMNXSV003027885
  • ILMN_1672879
  • ILMN_1764596
  • ILMN_1800096
  • PH_hs_0013192
  • PH_hs_0039227
  • TC22000275.hg
  • TC22001097.hg
  • X59434_at
  • g13489090_3p_s_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • THTM_HUMAN
  • A8MZ34
  • B3KP52
  • J3KPV7
  • O75750
  • Q6FHN9
sequenceLength 297
species [Species:48887] Homo sapiens
stId uniprot:P25325
url http://purl.uniprot.org/uniprot/P25325
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