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Literature summary for 1.8.1.14 extracted from

  • Herwald, S.; Liu, A.; Zhu, B.; Sea, K.; Lopez, K.; Sazinsky, M.; Crane, E.
    Structure and substrate specificity of the pyrococcal coenzyme A disulfide reductases/polysulfide reductases (CoADR/Psr). Implications for S(0)-based respiration and a sulfur-dependent antioxidant system in Pyrococcus (2013), Biochemistry, 52, 2764-2773 .
    View publication on PubMed
Search for more literature for 1.8.1.14

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3)pLysS Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging and sitting drop vapor diffusion method Pyrococcus horikoshii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0205
-
 CoA-disulfide pH 8.1, 50°C, cofactor: NADH Pyrococcus horikoshii
0.0562
-
 CoA-disulfide pH 8.1, 50°C, cofactor: NADPH Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58308
-
-
Pyrococcus horikoshii OT-3 O58308
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CoA-disulfide + NADH + H+ the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH, indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo Pyrococcus horikoshii 2 CoA + NAD+
-
 ?
CoA-disulfide + NADH + H+ the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH, indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo Pyrococcus horikoshii OT-3 2 CoA + NAD+
-
 ?
CoA-disulfide + NADPH + H+ the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH, indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo Pyrococcus horikoshii 2 CoA + NADP+
-
 ?
CoA-disulfide + NADPH + H+ the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH, indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo Pyrococcus horikoshii OT-3 2 CoA + NADP+
-
 ?
additional information catalyzes the NAD(P)Hdependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides Pyrococcus horikoshii ?
-
 ?
additional information catalyzes the NAD(P)Hdependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides Pyrococcus horikoshii OT-3 ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 48977, calculated from sequence Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
CoADR
-
 Pyrococcus horikoshii
coenzyme A disulfide reductase
-
 Pyrococcus horikoshii
PH0572
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 assay at Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.11
-
 CoA-disulfide pH 8.1, 50°C, cofactor: NADH Pyrococcus horikoshii
1.5
-
 CoA-disulfide pH 8.1, 50°C, cofactor: NADPH Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.1
-
 assay at Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
FAD binds 1 FAD per subunit Pyrococcus horikoshii
NADH the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH (depending on the oxidizing substrate), indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo Pyrococcus horikoshii
NADPH the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH (depending on the oxidizing substrate), indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo Pyrococcus horikoshii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
27
-
 CoA-disulfide pH 8.1, 50°C, cofactor: NADPH Pyrococcus horikoshii
54
-
 CoA-disulfide pH 8.1, 50°C, cofactor: NADH Pyrococcus horikoshii