1.2.7.11: 2-oxoacid oxidoreductase (ferredoxin)
This is an abbreviated version!
For detailed information about 2-oxoacid oxidoreductase (ferredoxin), go to the full flat file.
Word Map on EC 1.2.7.11
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1.2.7.11
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sulfolobus
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ferredoxins
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2-oxoacids
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thiamin
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thermoacidophilic
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pyrophosphate
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archaeon
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ofors
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pyruvate:ferredoxin
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2-oxoglutarate
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tpp
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iron-sulfur
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oxalate
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tokodaii
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2-oxobutyrate
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africanus
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halobium
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halobacterium
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2-oxoglutarate:ferredoxin
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analysis
- 1.2.7.11
- sulfolobus
- ferredoxins
- 2-oxoacids
- thiamin
-
thermoacidophilic
- pyrophosphate
- archaeon
-
ofors
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pyruvate:ferredoxin
- 2-oxoglutarate
- tpp
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iron-sulfur
- oxalate
- tokodaii
- 2-oxobutyrate
- africanus
- halobium
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halobacterium
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2-oxoglutarate:ferredoxin
- analysis
Reaction
+ + 2 oxidized ferredoxin = + + 2 reduced ferredoxin + 2 H+
Synonyms
2-ketoacid:ferredoxin oxidoreductase, 2-oxoacid: ferredoxin oxidoreductase, 2-oxoacid:ferredoxin oxidoreductase, 2-oxoacid:ferredoxin oxidoreductases, Ape1473/1472, KOR, OFOR, OFOR1, OFOR2, PFOR, Saci_2306, Saci_2307, StOFOR, StOFOR1, StOFOR2
ECTree
Advanced search results
Engineering
Engineering on EC 1.2.7.11 - 2-oxoacid oxidoreductase (ferredoxin)
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I255L
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kcat/Km for pyruvate is 11% of wild-type value, kcat/KM for 2-oxoglutarate is 21% of wild-type value
I255M
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kcat/Km for pyruvate is 13% of wild-type value, kcat/KM for 2-oxoglutarate is 2% of wild-type value
I255S
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kcat/Km for pyruvate is 23% of wild-type value, kcat/KM for 2-oxoglutarate is 35% of wild-type value
I255V
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kcat/Km for pyruvate is 14% of wild-type value, kcat/KM for 2-oxoglutarate is 38% of wild-type value
P254G
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kcat/Km for pyruvate is 12% of wild-type value, kcat/KM for 2-oxoglutarate is 20% of wild-type value
T256A
T256S
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kcat/Km for pyruvate is 15% of wild-type value, kcat/KM for 2-oxoglutarate is 92% of wild-type value
T256V
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kcat/Km for pyruvate is 17% of wild-type value, kcat/KM for 2-oxoglutarate is 68% of wild-type value
Y253F
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kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value
T256A
T256S
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kcat/Km for pyruvate is 15% of wild-type value, kcat/KM for 2-oxoglutarate is 92% of wild-type value
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T256V
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kcat/Km for pyruvate is 17% of wild-type value, kcat/KM for 2-oxoglutarate is 68% of wild-type value
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Y253F
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kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value
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C12A
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loss of ironsulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C15A
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loss of ironsulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C197A
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the enzyme retains an unidentified type of ironsulfur cluster
C46A
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loss of ironsulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
D468A
K125A
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the mutant enzyme shows a large increase in the Km-value for CoA and shows poor inactivation by 4-fluoro-7-nitrobenzofurazan, compared with K173A and wild type enzyme
K173A
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the mutant enzyme shows a large increase in the Km-value for CoA and shows poor inactivation by 4-fluoro-7-nitrobenzofurazan, compared with K173A and wild type enzyme
K49I
S41A
T349L
S41A
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the mutant shows reduced activity compared to the wild type enzyme
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T349L
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the mutant shows reduced activity compared to the wild type enzyme
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D468A
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mutant enzyme StOFOR1 with mutation D468A in alpha-subunit. Vmax with pyruvate as substrate is 1.3% compared to wild-type enzyme. No activity is detected with 2-oxoglutarate
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K49I
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mutant enzyme StOFOR1 with mutation K49I in alpha-subunit. Vmax with pyruvate as substrate is 28% compared to wild-type enzyme, Km with pyruvate as substrate is 2.8fold higher as compared to wild-type enzyme. No activity is detected with 2-oxoglutarate
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S41A
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mutant enzyme StOFOR1 with mutation S41A in alpha-subunit. Vmax with pyruvate as substrate is 29% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 40% compared to wild-type enzyme, Km with pyruvate as substrate is 1.5fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.5fold higher as compared to wild-type enzyme
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T349L
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mutant enzyme StOFOR1 with mutation T349L in alpha-subunit. Vmax with pyruvate as substrate is 43% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 74% compared to wild-type enzyme, Km with pyruvate as substrate is 1.6fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.1fold higher as compared to wild-type enzyme
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kcat and Km for 2-oxoglutarate are 33% and 51%, respectively, as compared with that of the wild-type enzyme
T256A
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kcat/Km for pyruvate is 21% of wild-type value, kcat/KM for 2-oxoglutarate is 15% of wild-type value
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kcat and Km for 2-oxoglutarate are 33% and 51%, respectively, as compared with that of the wild-type enzyme
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T256A
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kcat/Km for pyruvate is 21% of wild-type value, kcat/KM for 2-oxoglutarate is 15% of wild-type value
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mutant enzyme StOFOR1 with mutation D468A in alpha-subunit. Vmax with pyruvate as substrate is 1.3% compared to wild-type enzyme. No activity is detected with 2-oxoglutarate
D468A
inactive with 2-oxoglutarate and pyruvate as substrate
mutant enzyme StOFOR1 with mutation K49I in alpha-subunit. Vmax with pyruvate as substrate is 28% compared to wild-type enzyme, Km with pyruvate as substrate is 2.8fold higher as compared to wild-type enzyme. No activity is detected with 2-oxoglutarate
K49I
inactive with 2-oxoglutarate as substrate
the mutant shows reduced activity compared to the wild type enzyme
S41A
mutant enzyme StOFOR1 with mutation S41A in alpha-subunit. Vmax with pyruvate as substrate is 29% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 40% compared to wild-type enzyme, Km with pyruvate as substrate is 1.5fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.5fold higher as compared to wild-type enzyme
the mutant shows reduced activity compared to the wild type enzyme
T349L
mutant enzyme StOFOR1 with mutation T349L in alpha-subunit. Vmax with pyruvate as substrate is 43% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 74% compared to wild-type enzyme, Km with pyruvate as substrate is 1.6fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.1fold higher as compared to wild-type enzyme