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2-oxo-4-methylthiobutyrate + CoA + 2 methyl viologen
3-methylthiopropanoyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 48% of the activity compared to glyoxylate
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
2-oxoadipate + CoA + 2 methyl viologen
glutaryl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 49% of the activity compared to glyoxylate
-
-
?
2-oxobutanoate + CoA + 2 oxidized cytochrome c
propanoyl-CoA + CO2 + 2 reduced cytochrome c + 2 H+
-
-
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
2-oxoglutarate + CoA + 2 oxidized cytochrome c
succinyl-CoA + CO2 + 2 reduced cytochrome c + 2 H+
-
best substrate tested
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
2-oxoglutarate + CoA + 2 oxidized methyl viologen
succinyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 94% of the activity compared to glyoxylate
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
2-oxoglutarate + CoA + oxidized methyl viologen
succinoyl-CoA + CO2 + reduced methyl viologen
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen + H+
4-hydroxyphenylpyruvate + CoA + 2 methyl viologen
(4-hydroxyphenyl)acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 16% of the activity compared to glyoxylate
-
-
?
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
pyruvate + CoA + 2 oxidized methyl viologen
-
-
-
r
glyoxylate + CoA + 2 oxidized methyl viologen
formyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472
-
-
?
hydroxypyruvate + CoA + 2 methyl viologen
?
-
enzyme Ape1473/1472, 55% of the activity compared to glyoxylate
-
-
?
phenylpyruvate + CoA + 2 methyl viologen
phenylacetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
pyruvate + CoA + 2 oxidized cytochrome c
acetyl-CoA + CO2 + 2 reduced cytochrome c + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
pyruvate + CoA + oxidized methyl viologen
?
additional information
?
-
2-oxoacid + CoA + oxidized ferredoxin

acyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxoacid + CoA + oxidized ferredoxin
acyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen

propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
enzyme Ape1473/1472, 97% of the activity compared to glyoxylate
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
-
-
?
2-oxobutyrate + CoA + 2 oxidized methyl viologen
propanoyl-CoA + CO2 + 2 reduced methyl viologen
-
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin

propanoyl-CoA + CO2 + reduced ferredoxin
-
-
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
Sulfolobus solfataricus ferredoxin contains a dicluster, i.e., a [3Fe-4S] cluster and a [4Fe-4S] cluster, and to possibly contain one zinc center
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
Sulfolobus solfataricus ferredoxin contains a dicluster, i.e., a [3Fe-4S] cluster and a [4Fe-4S] cluster, and to possibly contain one zinc center
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
Sulfolobus solfataricus ferredoxin contains a dicluster, i.e., a [3Fe-4S] cluster and a [4Fe-4S] cluster, and to possibly contain one zinc center
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
kcat/Km for 2-oxobutyrate is 60% compared to the kcat/Km-value for pyruvate, recombinant wild-type enzyme
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
kcat/Km for 2-oxobutyrate is 60% compared to the kcat/Km-value for pyruvate, recombinant wild-type enzyme
-
-
?
2-oxobutyrate + CoA + oxidized ferredoxin
propanoyl-CoA + CO2 + reduced ferredoxin
-
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin

succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
specific activity under optimal conditions is 36% of the specific activity with 2-oxobutyrate
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 20.4% compared to 2-oxoglutarate, kcat/Km for 2-oxoglutarate is 6.5% compared to kcat/Km for 2-oxobutyrate
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 20.4% compared to 2-oxoglutarate, kcat/Km for 2-oxoglutarate is 6.5% compared to kcat/Km for 2-oxobutyrate
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 20.4% compared to 2-oxoglutarate, kcat/Km for 2-oxoglutarate is 6.5% compared to kcat/Km for 2-oxobutyrate
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
kcat/Km for 2-oxobutyrate is 12% of the kcat/Km-value for pyruvate, a cognate Zn-7Fe-ferredoxin serves as an electron acceptor
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
kcat/Km for 2-oxoglutarate is 12% compared to the kcat/Km-value for pyruvate, recombinant wild-type enzyme
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
kcat/Km for 2-oxoglutarate is 12% compared to the kcat/Km-value for pyruvate, recombinant wild-type enzyme
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
kcat/Km for 2-oxobutyrate is 12% of the kcat/Km-value for pyruvate, a cognate Zn-7Fe-ferredoxin serves as an electron acceptor
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the recombinant enzyme StOFOR2 exhibits a preference for pyruvate over 2-oxoglutarate. Because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the recombinant enzyme StOFOR2 exhibits a preference for pyruvate over 2-oxoglutarate. Because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
2-oxoglutarate + CoA + 2 oxidized ferredoxin
succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin

succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
?
2-oxoglutarate + CoA + oxidized ferredoxin
succinyl-CoA + CO2 + reduced ferredoxin + H+
-
-
-
?
2-oxoglutarate + CoA + oxidized methyl viologen

succinoyl-CoA + CO2 + reduced methyl viologen
-
-
-
r
2-oxoglutarate + CoA + oxidized methyl viologen
succinoyl-CoA + CO2 + reduced methyl viologen
-
-
-
r
2-oxoglutarate + CoA + oxidized methyl viologen

succinyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
?
2-oxoglutarate + CoA + oxidized methyl viologen
succinyl-CoA + CO2 + reduced methyl viologen + H+
-
-
-
?
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+

pyruvate + CoA + 2 oxidized ferredoxin
-
-
-
r
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
pyruvate + CoA + 2 oxidized ferredoxin
-
-
-
r
phenylpyruvate + CoA + 2 methyl viologen

phenylacetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 24% of the activity compared to glyoxylate
-
-
?
phenylpyruvate + CoA + 2 methyl viologen
phenylacetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 36% of the activity compared to glyoxylate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin

acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
specific activity under optimal conditions is 65% of the specific activity with 2-oxobutyrate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 31.2% compared to 2-oxoglutarate, kcat/Km for pyruvate is 19% compared to kcat/Km for 2-oxobutyrate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 31.2% compared to 2-oxoglutarate, kcat/Km for pyruvate is 19% compared to kcat/Km for 2-oxobutyrate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
relative activity is 31.2% compared to 2-oxoglutarate, kcat/Km for pyruvate is 19% compared to kcat/Km for 2-oxobutyrate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
r
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
r
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
a cognate Zn-7Fe-ferredoxin serves as an electron acceptor
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Vmax/Km is 1.9fold higher than that for 2-oxoglutarate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
a cognate Zn-7Fe-ferredoxin serves as an electron acceptor
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Vmax/Km is 1.9fold higher than that for 2-oxoglutarate
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
-
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
-
Lys125 in subunit b is the critical residue that interacts with CoA
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the recombinant enzyme StOFOR2 exhibits a preference for pyruvate over 2-oxoglutarate. The carboxylate group of pyruvate is recognized by Arg344 and Thr257 from the alpha-subunit of
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
the recombinant enzyme StOFOR2 exhibits a preference for pyruvate over 2-oxoglutarate. The carboxylate group of pyruvate is recognized by Arg344 and Thr257 from the alpha-subunit of
-
-
?
pyruvate + CoA + 2 oxidized ferredoxin
acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
because 2-oxoacid oxidoreductase enzymes from Sulfolobus tokodaii lack the intramolecular Fd-like domain V, there is a large pocket surrounded by domains III and VI in each protomer, which appears to be able to bind an external ferredoxin molecule
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen

acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
enzyme Ape1473/1472, 95% of the activity compared to glyoxylate
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
r
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
r
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
?
pyruvate + CoA + 2 oxidized methyl viologen
acetyl-CoA + CO2 + 2 reduced methyl viologen + 2 H+
-
-
-
?
pyruvate + CoA + oxidized methyl viologen

?
-
-
-
?
pyruvate + CoA + oxidized methyl viologen
?
-
-
-
?
additional information

?
-
-
Ape1473/1472 operates in the TCA cycle of Aeropyrum pernix
-
-
?
additional information
?
-
-
no activity with 3-methyl-2-oxovalerate, 4-methyl-2-oxovalerate, 2-oxoisocaproic acid or 2-oxooctanoic acid, enzyme Ape1473/1472
-
-
?
additional information
?
-
-
no activity with glyoxylate
-
-
?
additional information
?
-
-
enzyme displays broad substrate specificity toward 2-oxoacids, such as pyruvate, 2-oxobutanoate, and 2-oxoglutarate
-
-
?
additional information
?
-
-
no activity with glyoxylate
-
-
?
additional information
?
-
-
enzyme displays broad substrate specificity toward 2-oxoacids, such as pyruvate, 2-oxobutanoate, and 2-oxoglutarate
-
-
?
additional information
?
-
-
no activity with glyoxylate
-
-
?
additional information
?
-
-
enzyme displays broad substrate specificity toward 2-oxoacids, such as pyruvate, 2-oxobutanoate, and 2-oxoglutarate
-
-
?
additional information
?
-
enzyme is able to use low-potential ferredoxins of the green sulfur bacterium Chlorobium tepidum and of Sulfolobus acidocaldarius whereas CO2 fixation is not supported by the native ferredoxin of Desulfocurvibacter africanus. Methyl viologen as an artificial electron carrier also allows CO2 fixation
-
-
-
additional information
?
-
enzyme is able to use low-potential ferredoxins of the green sulfur bacterium Chlorobium tepidum and of Sulfolobus acidocaldarius whereas CO2 fixation is not supported by the native ferredoxin of Desulfocurvibacter africanus. Methyl viologen as an artificial electron carrier also allows CO2 fixation
-
-
-
additional information
?
-
-
the YPITP-motif is essential for the turnover of the reaction rather than the affinity toward 2-oxoacid
-
-
?
additional information
?
-
-
the YPITP-motif is essential for the turnover of the reaction rather than the affinity toward 2-oxoacid
-
-
?
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0.516
2-oxobutanoate
-
pH 7.0, 55°C
0.07 - 0.516
2-oxobutyrate
0.163 - 15
2-oxoglutarate
additional information
additional information
-
kinetic parameters of mutant enzymes
-
0.07
2-oxobutyrate

-
pH and temperature not specified in the publication
0.45
2-oxobutyrate
-
pH 7.5, 80°C, recombinant wild-type enzyme
0.48
2-oxobutyrate
-
pH 7.5, 80°C, natural enzyme
0.516
2-oxobutyrate
-
pH 7.0, 55°C
0.163
2-oxoglutarate

-
pH 7.0, 55°C
0.33
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme T256V
0.37
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme T256A
0.5
2-oxoglutarate
-
pH 8.5, 80°C, enzyme Ape1473/1472
0.72
2-oxoglutarate
-
pH 7.5, 80°C, recombinant enzyme
0.85
2-oxoglutarate
-
pH 7.5, 80°C, natural enzyme
0.85
2-oxoglutarate
-
pH 7.5, 80°C, recombinant wild-type enzyme
0.87
2-oxoglutarate
pH 6.8, 50°C
0.87
2-oxoglutarate
pH and temperature not specified in the publication
0.87
2-oxoglutarate
-
pH 7.5, 80°C, natural enzyme
0.89
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme I255S
1.1
2-oxoglutarate
-
pH and temperature not specified in the publication
1.1
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme I255L
1.2
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme P254G
1.3
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme I255M
1.5
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme P253F
2.1
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme T256S
2.1
2-oxoglutarate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, enzyme StOFOR1
2.1
2-oxoglutarate
wild type enzyme, at pH 8.5 and 80°C
2.3
2-oxoglutarate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation T349L in alpha-subunit
2.3
2-oxoglutarate
mutant enzyme T349L, at pH 8.5 and 80°C
3.2
2-oxoglutarate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation S41A in alpha-subunit
3.2
2-oxoglutarate
mutant enzyme S41A, at pH 8.5 and 80°C
3.3
2-oxoglutarate
-
pH 7.5, 80°C, mutant enzyme I255V
15
2-oxoglutarate
pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, enzyme StOFOR2
15
2-oxoglutarate
wild type enzyme, at pH 8.5 and 80°C
0.05
CoA

-
pH 8.5, 80°C, mutant enzyme K173A
0.074
CoA
-
pH 8.5, 80°C, wild-type enzyme
1.17
CoA
-
pH 8.5, 80°C, mutant enzyme K125A
0.07
oxidized ferredoxin

-
cosubstrates: 1 mM 2-oxoxbutyrate, 0.05 mM CoA, pH and temperature not specified in the publication
0.07
oxidized ferredoxin
-
cosubstrates: 1 mM pyruvate, 0.05 mM CoA, pH and temperature not specified in the publication
0.1
pyruvate

-
pH and temperature not specified in the publication
0.11
pyruvate
-
pH 7.5, 80°C, mutant enzyme T256S