1.18.1.5: putidaredoxin-NAD+ reductase
This is an abbreviated version!
For detailed information about putidaredoxin-NAD+ reductase, go to the full flat file.
Word Map on EC 1.18.1.5
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1.18.1.5
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p450cam
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self-sufficient
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skinfolds
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5-exo-hydroxycamphor
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peucetius
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synthesis
- 1.18.1.5
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p450cam
-
self-sufficient
-
skinfolds
- 5-exo-hydroxycamphor
- peucetius
- synthesis
Reaction
Synonyms
camA, Pdr, putidaredoxin reductase
ECTree
1.18.1.5 putidaredoxin-NAD+ reductaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.18.1.5 - putidaredoxin-NAD+ reductase
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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
NADH + H+ + oxidized 2,6-dichlorophenolindophenol
NAD+ + reduced 2,6-dichlorophenolindophenol
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?
reduced 2,6-dichlorophenolindophenol + NAD+
oxidized 2,6-dichlorophenolindophenol + NADH + H+
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?
reduced putidaredoxin + ferricytochrome c
oxidized putidaredoxin + ferrocytochrome c
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the physiological electron acceptor, putidaredoxin, can be used to transfer electrons to ferri-cytochrome c in a putidaredoxin-dependent cytochrome c reductase assay
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?
reduced putidaredoxin + NAD+
oxidized putidaredoxin + NADH + H+
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?
reduced putidaredoxin + NAD+
oxidized putidaredoxin + NADH + H+
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?
additional information
?
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bulky side chains of Tyr33, Arg66, and Trp106 prevent tight binding of oxidized Pdx and facilitate dissociation of the reduced iron-sulfur protein from Pdr. Transfer of an electron from FAD to [2Fe-2S] can occur with various orientations between the cofactors through multiple electron transfer pathways that do not involve Trp106 but are likely to include Asp38 and Cys39
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?
additional information
?
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bulky side chains of Tyr33, Arg66, and Trp106 prevent tight binding of oxidized Pdx and facilitate dissociation of the reduced iron-sulfur protein from Pdr. Transfer of an electron from FAD to [2Fe-2S] can occur with various orientations between the cofactors through multiple electron transfer pathways that do not involve Trp106 but are likely to include Asp38 and Cys39
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?
additional information
?
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reductase is a two-eleetron acceptor with no stable semiquinone intermediate being formed either during reduction or air reoxidation
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?
additional information
?
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the midpoint oxidation-reduction potential of PdR is -369 mV at pH 7.6, which is more negative than the pyridine nucleotide NADH/NAD+. The midpoint potential is a hyperbolic function of increasing NAD+ concentration, such that at concentrations of pyridine nucleotide typically found in an intracellular environment, the midpoint potential would be -230 mV, thereby providing the thermodynamically favorable redox equilibria that enables electron transfer from NADH, with thermodynamic control of electron transfer. The PdRox:NAD+ complex is about 5 orders of magnitude weaker than PdRrd:NAD+ binding. These results support a compulsory ordered pathway to describe the electron-transfer processes
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?
additional information
?
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wild-type and His6 Pdr are able to function as NAD(H)-dependent dithiol/disulfide oxidoreductases catalyzing both forward and reverse reactions, NAD+-dependent oxidation of thiols, and NADH-dependent reduction of disulfides. This function of the flavoprotein can be dissociated from electron transfer to putidaredoxin
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?
additional information
?
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wild-type and His6 Pdr are able to function as NAD(H)-dependent dithiol/disulfide oxidoreductases catalyzing both forward and reverse reactions, NAD+-dependent oxidation of thiols, and NADH-dependent reduction of disulfides. This function of the flavoprotein can be dissociated from electron transfer to putidaredoxin
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?
