Any feedback?
Information on EC 2.8.1.2 - 3-mercaptopyruvate sulfurtransferase and Organism(s) Escherichia coli and UniProt Accession P31142
for references in articles please use BRENDA:EC2.8.1.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.8.1.2 3-mercaptopyruvate sulfurtransferaseIUBMB Comments
The enzyme catalyses a transsulfuration reaction from 2-oxo-3-sulfanylpropanoate to an internal cysteine residue. In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide. The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11).
Specify your search results
Word Map
- 2.8.1.2
- h2s
- cystathionine
- rhodanese
-
h2s-producing
- thiosulfate
-
gaseous
-
gasotransmitter
-
sulfane
- nahs
- polysulfides
- persulfide
-
cytoprotective
-
h2s-synthesizing
- beta-synthase
-
desulfuration
-
h2s-generating
- d-cysteine
-
gamma-lyase
- analysis
-
trisulfide
-
aminooxyacetic
-
sulfhydration
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
3-mercaptopyruvate sulfurtransferase, 3-mst, mercaptopyruvate sulfurtransferase, 3-mercaptopyruvate sulphurtransferase, 3-mpst, 3-mercaptopyruvate:cyanide sulfurtransferase, beta-mercaptopyruvate sulfurtransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-MPST
-
-
-
-
beta-mercaptopyruvate sulfurtransferase
-
-
-
-
beta-mercaptopyruvate trans-sulfurase
-
-
-
-
SseA
-
-
-
-
sulfurtransferase, 3-mercaptopyruvate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
mechanism
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
sulfur transfer mechanism involving C237 as the nucleophilic species and H66, R102 and D262 as residues assisting catalysis
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3-mercaptopyruvate:cyanide sulfurtransferase
The enzyme catalyses a transsulfuration reaction from 2-oxo-3-sulfanylpropanoate to an internal cysteine residue. In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide. The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11).
CAS REGISTRY NUMBER
COMMENTARY
9026-05-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
-
no effect: 0.02 M CdCl2, 0.5 mM arsenite, 0.01 mM copper acetate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyanide
-
inhibits at short-time intervals, slight enhancement at longer periods
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.34
3-Mercaptopyruvate
-
determination of pyruvate formation, 37°C, pH 9.55
12.5
3-Mercaptopyruvate
-
determination of thiocyanate formation, 37°C, pH 9.55
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the first step of sulfur transfer that leads to pyruvate release and formation of the persulfide intermediate is very efficient. It critically depends on the electrostatic contribution provided by the CGSGVT catalytic loop, any role of the so-called Ser/His/Asp triad can be excluded. In a concerted mechanism, the water-mediated protonation of the pyruvate enolate and S0 transfer from the deprotonated 3-mercaptopyruvate to the thiolate form of the catalytic cysteine occur concomitantly
physiological function
-
cysteine desulfurase (IscS, EC 2.8.1.7), not 3-MST, is the primary source of endogenous H2S in Escherichia coli under anaerobic conditions. A significant decrease in H2S production under anaerobic conditions is observed in Escherichia coli upon deletion of IscS, but not in 3-MST-deficient bacteria
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D53A
-
mutation of catalytic triad, does not change the kinetic parameters of for the first reaction step
H66A
-
the first step of sulfur transfer becomes rate-limiting in the mutant
H66A/R102L
-
the first step of sulfur transfer becomes rate-limiting in the mutant, with cumulative effects of the mutations
R102K
-
the first step of sulfur transfer becomes rate-limiting in the mutant
R102L
-
the first step of sulfur transfer becomes rate-limiting in the mutant
R178L
-
moderate decrease in kmax1/K3-mercaptopyruvate, the first step of sulfur transfer is not drastically impaired
R178L/R187L
-
substituting both Arg residues does not fully abolish the sulfur transfer step
R187L
-
moderate decrease in kmax1/K3-mercaptopyruvate, the first step of sulfur transfer is not drastically impaired
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against urea inactivates, effect is reversed by dialysis, dilution or electrophoresis
-
markedly stabilized during purification and storage by the presence of monovalent cations, maximal stability is obtained if purification and storage are carried out at pH 6.5-7.5 in presence of 0.8 M KCl and 2 mM 2-mercaptoethanol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vachek, H.; Wood, J.L.
Purification and properties of mercaptopyruvate sulfur transferase of Escherichia coli
Biochim. Biophys. Acta
258
133-146
1972
Escherichia coli
Spallarossa, A.; Forlani, F.; Carpen, A.; Armirotti, A.; Pagani, S.; Bolognesi, M.; Bordo, D.
The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: Crystal structure of SseA from Escherichia coli
J. Mol. Biol.
335
583-593
2004
Escherichia coli (P31142)
Lec, J.; Boutserin, S.; Mazon, H.; Mulliert, G.; Boschi-Muller, S.; Talfournier, F.
Unraveling the mechanism of cysteine persulfide formation catalyzed by 3-mercaptopyruvate sulfurtransferases
ACS Catal.
8
2049-2059
2018
Escherichia coli, Homo sapiens (P25325), Escherichia coli DH5alpha
-
Wang, J.; Guo, X.; Li, H.; Qi, H.; Qian, J.; Yan, S.; Shi, J.; Niu, W.
Hydrogen sulfide from cysteine desulfurase, not 3-mercaptopyruvate sulfurtransferase, contributes to sustaining cell growth and bioenergetics in E. coli under anaerobic conditions
Front. Microbiol.
10
2357
2019
Escherichia coli, Escherichia coli BW25113
EXTERNAL LINKS (specific for EC-Number 2.8.1.2)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
