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Literature summary for 1.8.1.14 extracted from

  • Sea, K.; Lee, J.; To, D.; Chen, B.; Sazinsky, M.H.; Crane, E.J.
    A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry (2018), FEBS open bio, 8, 1083-1092 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.1.14

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method at room temperature Pyrococcus horikoshii

Protein Variants

Protein Variants Comment Organism
Y65A/Y66A/P67G/H367G the structure of the quadruple mutant shows a widened substrate channel, which is supported by a fourfold increase in kcat for the NAD(P)H-dependent reduction of CoA disulfide and enhanced activity toward the substrate at lower temperatures Pyrococcus horikoshii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0164
-
 NADPH pH 7.5, 75°C, mutant enzyme Y65A/Y66A/P67G/H367G Pyrococcus horikoshii
0.0286
-
 CoA-disulfide pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, wild-type enzyme Pyrococcus horikoshii
0.052
-
 CoA-disulfide pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, wild-type enzyme Pyrococcus horikoshii
0.057
-
 CoA-disulfide pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, mutant enzyme Y65A/Y66A/P67G/H367G Pyrococcus horikoshii
0.073
-
 NADH pH 7.5, 75°C, wild-type enzyme Pyrococcus horikoshii
0.075
-
 NADH pH 7.5, 75°C, mutant enzyme Y65A/Y66A/P67G/H367G Pyrococcus horikoshii
0.086
-
 CoA-disulfide pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, mutant enzyme Y65A/Y66A/P67G/H367G Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58308
-
-
Pyrococcus horikoshii ATCC 700860 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 phCoADR structure has a narrower access channel for CoA substrates, which suggests that this restriction might be responsible for the poor activity toward the bulky CoA disulfide substrate Pyrococcus horikoshii 2 CoA + NAD+
-
 ?
CoA-disulfide + NADH + H+ the phCoADR structure has a narrower access channel for CoA substrates, which suggests that this restriction might be responsible for the poor activity toward the bulky CoA disulfide substrate Pyrococcus horikoshii ATCC 700860 2 CoA + NAD+
-
 ?
CoA-disulfide + NADPH + H+ the phCoADR structure has a narrower access channel for CoA substrates, which suggests that this restriction might be responsible for the poor activity toward the bulky CoA disulfide substrate Pyrococcus horikoshii 2 CoA + NADP+
-
 ?
CoA-disulfide + NADPH + H+ the phCoADR structure has a narrower access channel for CoA substrates, which suggests that this restriction might be responsible for the poor activity toward the bulky CoA disulfide substrate Pyrococcus horikoshii ATCC 700860 2 CoA + NADP+
-
 ?

Subunits

Subunits Comment Organism
homodimer
-
 Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
CoADR
-
 Pyrococcus horikoshii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.8
-
 CoA-disulfide pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, mutant enzyme Y65A/Y66A/P67G/H367G Pyrococcus horikoshii
2.3
-
 NADH pH 7.5, 75°C, wild-type enzyme Pyrococcus horikoshii
4.4
-
 CoA-disulfide pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, wild-type enzyme Pyrococcus horikoshii
5.43
-
 CoA-disulfide pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, wild-type enzyme Pyrococcus horikoshii
5.8
-
 NADPH pH 7.5, 75°C, wild-type enzyme Pyrococcus horikoshii
8.1
-
 NADH pH 7.5, 75°C, mutant enzyme Y65A/Y66A/P67G/H367G Pyrococcus horikoshii
18.8
-
 CoA-disulfide pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, mutant enzyme Y65A/Y66A/P67G/H367G Pyrococcus horikoshii
21.6
-
 NADPH pH 7.5, 75°C, mutant enzyme Y65A/Y66A/P67G/H367G Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
FAD FAD-dependent reductase Pyrococcus horikoshii