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
-
p450cam
-
self-sufficient
-
skinfolds
- 5-exo-hydroxycamphor
- peucetius
- synthesis
Reaction
Synonyms
camA, Pdr, putidaredoxin reductase
ECTree
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Subunits
Subunits on EC 1.18.1.5 - putidaredoxin-NAD+ reductase
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dimer
monomer
both WT and His6-Pdr undergo a monomer-dimer association-dissociation
additional information
dimer
both WT and His6-Pdr undergo a monomer-dimer association-dissociation
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cross-linking of putidaredoxin and putidaredoxin reductase by 1-ethyl 3-[3-(dimethylamino)propyl]carbodiimide, EDC. EDC promotes formation of stoichiometric Pdr-Pdx complexes only when carboxyl groups on putidaredoxin are activated. The putidaredoxin-putidaredoxin reductase C73S/C85S conjugate protein is more efficient in electron transfer to cytochrome c and, in the presence of saturating levels of P450cam, more effectively supports camphor hydroxylation. The cross-linked complex is physiologically relevant and represents a suitable model for mechanistic studies, and molecular recognition between putidaredoxin and putidaredoxin reductase is redox-controlled and assisted by the putidaredoxin Glu72 and putidaredoxin reducase Lys409 charge-charge interactions
additional information
Pdr-Pdx complex formation is mainly driven by steric complementarity, 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
additional information
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Pdr-Pdx complex formation is mainly driven by steric complementarity, 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