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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

Reaction

a 2-oxocarboxylate
+
CoA
+ 2 oxidized ferredoxin =
an acyl-CoA
+
CO2
+ 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

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.7 With an iron-sulfur protein as acceptor
                1.2.7.11 2-oxoacid oxidoreductase (ferredoxin)

Engineering

Engineering on EC 1.2.7.11 - 2-oxoacid oxidoreductase (ferredoxin)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I255L
-
kcat/Km for pyruvate is 11% of wild-type value, kcat/KM for 2-oxoglutarate is 21% of wild-type value
I255M
-
kcat/Km for pyruvate is 13% of wild-type value, kcat/KM for 2-oxoglutarate is 2% of wild-type value
I255S
-
kcat/Km for pyruvate is 23% of wild-type value, kcat/KM for 2-oxoglutarate is 35% of wild-type value
I255V
-
kcat/Km for pyruvate is 14% of wild-type value, kcat/KM for 2-oxoglutarate is 38% of wild-type value
P254G
-
kcat/Km for pyruvate is 12% of wild-type value, kcat/KM for 2-oxoglutarate is 20% of wild-type value
P257A
-
no enzyme activity at either 50 or 80°C
P257G
-
no enzyme activity at either 50 or 80°C
P257V
-
no enzyme activity at either 50 or 80°C
T256A
T256S
-
kcat/Km for pyruvate is 15% of wild-type value, kcat/KM for 2-oxoglutarate is 92% of wild-type value
T256V
-
kcat/Km for pyruvate is 17% of wild-type value, kcat/KM for 2-oxoglutarate is 68% of wild-type value
Y253A
-
no enzyme activity at either 50 or 80°C
Y253F
-
kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value
Y253W
-
no enzyme activity at either 50 or 80°C
T256A
T256S
-
kcat/Km for pyruvate is 15% of wild-type value, kcat/KM for 2-oxoglutarate is 92% of wild-type value
-
T256V
-
kcat/Km for pyruvate is 17% of wild-type value, kcat/KM for 2-oxoglutarate is 68% of wild-type value
-
Y253F
-
kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value
-
C12/15A
-
loss of iron–sulfur cluster
C12A
-
loss of iron–sulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C15A
-
loss of iron–sulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
C197A
-
the enzyme retains an unidentified type of iron–sulfur cluster
C46A
-
loss of iron–sulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA
D468A
K125A
-
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
-
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
T349L
D468A
-
inactive with 2-oxoglutarate and pyruvate as substrate
-
K49I
-
inactive with 2-oxoglutarate as substrate
-
S41A
-
the mutant shows reduced activity compared to the wild type enzyme
-
T349L
-
the mutant shows reduced activity compared to the wild type enzyme
-
D468A
-
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
-
K49I
-
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
-
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
-
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
-