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 (Engineering
Engineering on EC 1.18.1.5 - putidaredoxin-NAD+ reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C73G
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surface mutation facilitating crystallization without affecting cluster ligation and with only minor effects on activity
C73S
mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx
C73S/C85S
mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx
C85S
mutation improves protein stability. Decreasing order of stability is C73S/C85S, C73S, C85S, wild-type Pdx
D38A
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 45% of wild-type activity
D38N
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 33% of wild-type activity
K339A
moderate decrease in the binding affinity and reduction of Pdx
K387A
moderate decrease in the binding affinity and reduction of Pdx
K409A
moderate decrease in the binding affinity and reduction of Pdx
R310A
mutation lowers the interprotein electron tranfer rate by 20-30fold without perturbing the Pdx association step
R310E
mutation decreases both the Pdr-to-Pdx ET and partner binding affinity by 100- and 8fold, respectively
R65A
mutation lowers the interprotein electron tranfer rate by 20-30fold without perturbing the Pdx association step
R66A
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 25% of wild-type activity
R66E
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 21% of wild-type activity
W106A
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 54% of wild-type activity
W106Delta
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 102% of wild-type activity
W106F
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 83% of wild-type activity
Y33A
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 26% of wild-type activity
Y33F
mutation does not affect assembly of the [2Fe-2S] cluster and results in a marginal change in the redox potential of Pdx. 21% of wild-type activity
additional information
additional information
expression of wild-type as His-tagged protein. Molecular, spectral, and electron transferring properties of recombinant His6-Pdr to artificial and native electron acceptors are similar to those of the wild-type protein. Contrary to wild-type, under anaerobic conditions, NAD+ induces in His6 Pdr spectral changes indicative of flavin reduction and formation of the charge transfer complex between the reduced FAD and NAD+
additional information
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expression of wild-type as His-tagged protein. Molecular, spectral, and electron transferring properties of recombinant His6-Pdr to artificial and native electron acceptors are similar to those of the wild-type protein. Contrary to wild-type, under anaerobic conditions, NAD+ induces in His6 Pdr spectral changes indicative of flavin reduction and formation of the charge transfer complex between the reduced FAD and NAD+
additional information
for expression in Escherichia coli, change of the rare start codon, GTG, results in an 18fold increase in the level of expression of the protein to 7.4 mg/g wet weight of cells
additional information
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for expression in Escherichia coli, change of the rare start codon, GTG, results in an 18fold increase in the level of expression of the protein to 7.4 mg/g wet weight of cells
additional information
functional expression in Escherichia coli of tricistronic constructs consisting of P450cam and the auxiliary proteins, Pd and PdR. Transformed bacterial whole cells efficiently oxidize (1R)-(+)-camphor to 5-exo-hydroxycamphor and interestingly limonene to (-)-perillyl alcohol. These bioengineered Escherichia coli cells possess a heterologous selfsufficient P450 catalytic system
additional information
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functional expression in Escherichia coli of tricistronic constructs consisting of P450cam and the auxiliary proteins, Pd and PdR. Transformed bacterial whole cells efficiently oxidize (1R)-(+)-camphor to 5-exo-hydroxycamphor and interestingly limonene to (-)-perillyl alcohol. These bioengineered Escherichia coli cells possess a heterologous selfsufficient P450 catalytic system
