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Literature summary extracted from

  • 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 (2018), ACS Catal., 8, 2049-2059 .
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
2.8.1.2 D53A mutation of catalytic triad, does not change the kinetic parameters of for the first reaction step Escherichia coli
2.8.1.2 H66A 10fold decrease in kmax1/K3-mercaptopyruvate ratio relative to the wild-type Homo sapiens
2.8.1.2 H66A the first step of sulfur transfer becomes rate-limiting in the mutant Escherichia coli
2.8.1.2 H66A/R102L the first step of sulfur transfer becomes rate-limiting in the mutant, with cumulative effects of the mutations Escherichia coli
2.8.1.2 H66N kinetic properties are identical with those of the wild type Escherichia coli
2.8.1.2 R102K the first step of sulfur transfer becomes rate-limiting in the mutant Escherichia coli
2.8.1.2 R102L the first step of sulfur transfer becomes rate-limiting in the mutant Escherichia coli
2.8.1.2 R178L moderate decrease in kmax1/K3-mercaptopyruvate, the first step of sulfur transfer is not drastically impaired Escherichia coli
2.8.1.2 R178L/R187L substituting both Arg residues does not fully abolish the sulfur transfer step Escherichia coli
2.8.1.2 R187L moderate decrease in kmax1/K3-mercaptopyruvate, the first step of sulfur transfer is not drastically impaired Escherichia coli
2.8.1.2 S239A strong decrease in kcat value Escherichia coli
2.8.1.2 S239A no key role of residue S239 in the activation of the 3-mercaptopyruvate thiol group Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.8.1.2 0.24
-
 3-Mercaptopyruvate mutant S239A, pH 8.0, 30°C Escherichia coli
2.8.1.2 0.43
-
 3-Mercaptopyruvate mutant H66A, pH 8.0, 30°C Escherichia coli
2.8.1.2 0.6
-
 3-Mercaptopyruvate mutant S239A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C Homo sapiens
2.8.1.2 0.79
-
 3-Mercaptopyruvate mutant H66A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C Homo sapiens
2.8.1.2 0.9
-
 3-Mercaptopyruvate mutant R102L, pH 8.0, 30°C Escherichia coli
2.8.1.2 1
-
 3-Mercaptopyruvate wild-type, pH 8.0, 30°C Escherichia coli
2.8.1.2 1
-
 3-Mercaptopyruvate mutant H66A/R102L, pH 8.0, 30°C Escherichia coli
2.8.1.2 1
-
 3-Mercaptopyruvate mutant R102K, pH 8.0, 30°C Escherichia coli
2.8.1.2 1.4
-
 3-Mercaptopyruvate mutant H66N, pH 8.0, 30°C Escherichia coli
2.8.1.2 1.7
-
 3-Mercaptopyruvate wild-type, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C Homo sapiens
2.8.1.2 2 3 3-Mercaptopyruvate mutant R178L/R187L, pH 8.0, 30°C Escherichia coli
2.8.1.2 2.4
-
 3-Mercaptopyruvate mutant D53A, pH 8.0, 30°C Escherichia coli
2.8.1.2 4
-
 3-Mercaptopyruvate mutant R187L, pH 8.0, 30°C Escherichia coli
2.8.1.2 15
-
 3-Mercaptopyruvate mutant R178L, pH 8.0, 30°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.2 Escherichia coli
-
-
-
2.8.1.2 Escherichia coli DH5alpha
-
-
-
2.8.1.2 Homo sapiens P25325
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.2 3-mercaptopyruvate + thioredoxin
-
 Escherichia coli pyruvate + persulfurated thioredoxin
-
 ?
2.8.1.2 3-mercaptopyruvate + thioredoxin
-
 Homo sapiens pyruvate + persulfurated thioredoxin
-
 ?
2.8.1.2 3-mercaptopyruvate + thioredoxin
-
 Escherichia coli DH5alpha pyruvate + persulfurated thioredoxin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.8.1.2 MPST
-
 Escherichia coli
2.8.1.2 MPST
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.8.1.2 0.05
-
 3-Mercaptopyruvate mutant R178L, pH 8.0, 30°C Escherichia coli
2.8.1.2 0.068
-
 3-Mercaptopyruvate mutant R178L/R187L, pH 8.0, 30°C Escherichia coli
2.8.1.2 0.11
-
 3-Mercaptopyruvate mutant S239A, pH 8.0, 30°C Homo sapiens
2.8.1.2 0.16
-
 3-Mercaptopyruvate mutant R187L, pH 8.0, 30°C Escherichia coli
2.8.1.2 0.47
-
 3-Mercaptopyruvate wild-type, pH 8.0, 30°C Homo sapiens
2.8.1.2 0.48
-
 3-Mercaptopyruvate mutant H66A, pH 8.0, 30°C Homo sapiens
2.8.1.2 1
-
 3-Mercaptopyruvate mutant D53A, pH 8.0, 30°C Escherichia coli
2.8.1.2 2.5
-
 3-Mercaptopyruvate mutant S239A, pH 8.0, 30°C Escherichia coli
2.8.1.2 3.9
-
 3-Mercaptopyruvate mutant H66A/R102L, pH 8.0, 30°C Escherichia coli
2.8.1.2 20
-
 3-Mercaptopyruvate mutant H66A, pH 8.0, 30°C Escherichia coli
2.8.1.2 49
-
 3-Mercaptopyruvate mutant R102L, pH 8.0, 30°C Escherichia coli
2.8.1.2 59
-
 3-Mercaptopyruvate mutant R102K, pH 8.0, 30°C Escherichia coli
2.8.1.2 75
-
 3-Mercaptopyruvate mutant H66N, pH 8.0, 30°C Escherichia coli
2.8.1.2 112
-
 3-Mercaptopyruvate wild-type, pH 8.0, 30°C Escherichia coli

General Information

EC Number General Information Comment Organism
2.8.1.2 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 Escherichia coli
2.8.1.2 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 Homo sapiens