1.3.8.17: dehydro coenzyme F420 reductase
This is an abbreviated version!
For detailed information about dehydro coenzyme F420 reductase, go to the full flat file.
Reaction
Synonyms
bifunctional F420 biosynthesis protein FbiB, BQ2027_MB3290, FbiB, mftC, mycofactocin maturase, WP_052294161
ECTree
1.3.8.17 dehydro coenzyme F420 reductaseAdvanced search results
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results (Engineering
Engineering on EC 1.3.8.17 - dehydro coenzyme F420 reductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C269A
auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo but incapable of converting MftA to MftA* or MftA**
C30A/C37A
radical S-adenosylmethionine mutant, can neither cleave SAM nor modify MftA
C310A/C341A
auxiliary [4Fe-4S] cluster II mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo, incapable of converting MftA to MftA* or MftA**
C323A
auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo, incapable of converting MftA to MftA* or MftA**
C269A
-
auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo but incapable of converting MftA to MftA* or MftA**
-
C30A/C37A
-
radical S-adenosylmethionine mutant, can neither cleave SAM nor modify MftA
-
C323A
-
auxiliary [4Fe-4S] cluster I mutant, capable of catalyzing the reductive cleavage of SAM to form dAdo, incapable of converting MftA to MftA* or MftA**
-
additional information
additional information
systematical replacement of Cys residues by Ala. The RS KO could neither cleave SAM nor modify MftA, consistent with the successful knockout of the RS cluster. Activity assays for Aux I and Aux II KO's also provided insightful results. Both Aux I and Aux II KO's were capable of catalyzing the reductive cleavage of SAM to form dAdo (Figure 3A), suggesting that the RS cluster remained intact and in an active conformation in the mutated proteins. However, when assayed against MftA, both Aux I and Aux II KO's were incapable of converting MftA to MftA* or MftA**
additional information
-
systematical replacement of Cys residues by Ala. The RS KO could neither cleave SAM nor modify MftA, consistent with the successful knockout of the RS cluster. Activity assays for Aux I and Aux II KO's also provided insightful results. Both Aux I and Aux II KO's were capable of catalyzing the reductive cleavage of SAM to form dAdo (Figure 3A), suggesting that the RS cluster remained intact and in an active conformation in the mutated proteins. However, when assayed against MftA, both Aux I and Aux II KO's were incapable of converting MftA to MftA* or MftA**
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