Information on EC 1.2.7.8 - indolepyruvate ferredoxin oxidoreductase

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indolepyruvate:Fd oxidoreductase

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IOR

4 entries

phenylpyruvate oxidase

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VOR

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phenylalanine metabolism, tryptophan metabolism

(indol-3-yl)pyruvate + CoA + 2 oxidized ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+

this enzyme, which is found in archaea, is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see aslo EC 1.2.7.1, pyruvate synthase, EC 1.2.7.7., 2-oxoisovalerate ferredoxin reductase and EC 1.2.7.9, 2-oxoglutarate ferredoxin oxidoreductase). Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates

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oxidative decarboxylation

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BRENDA

3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating)

Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).

158886-06-7

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(indol-3-yl)pyruvate + CoA + oxidized ferredoxin

S-2-(indol-3-yl)acetyl-CoA + CO2 + 2 reduced ferredoxin + H+

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Substrates: -
Products: -

r

(indol-3-yl)pyruvate + CoA + oxidized ferredoxin

S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin

(indol-3-yl)pyruvate + CoA + oxidized ferredoxin

S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+

2-keto-4-methylthiobutyrate + CoA + oxidized ferredoxin

CO2 + reduced ferredoxin + 3-methylthiopropionyl-CoA

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Substrates: -
Products: -

r

2-ketoisocaproate + CoA + oxidized ferredoxin

CO2 + reduced ferredoxin + isovaleryl-CoA

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Substrates: -
Products: -

r

3-methyl-2-oxobutanoate + H2O + oxidized methyl viologen

S-(2-methylpropanoyl)-CoA + reduced methyl viologen + H+

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Substrates: -
Products: -

?

4-hydroxyphenylpyruvate + CoA + oxidized ferredoxin

4-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin + H+

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Substrates: -
Products: -

?

4-hydroxyphenylpyruvate + CoA + oxidized ferredoxin

? + CO2 + reduced ferredoxin + H+

indolepyruvate + CoA + oxidized methylviologen

indoleacetyl-CoA + CO2 + reduced methylviologen

4 entries

p-hydroxyphenylpyruvate + CoA + oxidized ferredoxin

p-hydroxyphenylacetyl-CoA + CO2 + reduced ferredoxin

phenylpyruvate + CoA + oxidized ferredoxin

phenylacetyl-CoA + CO2 + reduced ferredoxin

phenylpyruvate + CoA + oxidized methyl viologen

phenylacetyl-CoA + CO2 + reduced methyl viologen + H+

additional information

?

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(indol-3-yl)pyruvate + CoA + oxidized ferredoxin

S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin

(indol-3-yl)pyruvate + CoA + oxidized ferredoxin

S-2-(indol-3-yl)acetyl-CoA + CO2 + reduced ferredoxin + H+

Ferredoxin

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Km-value 0.06 mM

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[4Fe-4S]-center

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Cu2+

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cyanide

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KCN

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Zn2+

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additional information

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not inhibited by CO, unaffected by sodium nitrite, not inhibited by sodium fluoride or sodium azide, sodium benzoate, phenylacetate, pyruvate, 2-ketoglutarate and oxamate have no effect on activity

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thiamine diphosphate

0.22

(indol-3-yl)pyruvate

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in 50 mM TAPS buffer (pH 9.0), at 80°C

0.13

4-hydroxyphenylpyruvate

0.015 - 0.021

CoA

0.048

Ferredoxin

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639362

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0.22 - 0.25

Indolepyruvate

0.048 - 0.06

oxidized ferredoxin

0.11

p-hydroxyphenylpyruvate

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pH 8.4, 80°C

0.018 - 1.4

phenylpyruvate

4 entries

7.5

KCN

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pH 8.4, 80°C

1.01

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cell-free extract, in 50 mM TAPS buffer (pH 9.0), at 80°C

121

Methanothermobacter thermautotrophicus

31.15

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644697

38

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87

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74fold purified enzyme, purified by an effective affinity chromatography technique

Methanothermobacter thermautotrophicus

10

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644697

8.5 - 10.5

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at 80°C

105

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70

80

90

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exhibits optimal activity above at pH 8.0

20 - 30

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negligible activity

45 - 80

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644703

60 - 100

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dramatic increase of activity

70 - 90

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shows dramatic increase in activity above 70°C

Methanococcus maripaludis

Methanothermobacter thermautotrophicus

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639362, 644697

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Methanothermobacter thermautotrophicus Marburg / DSM 2133

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644697

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Thermococcus profundus DSM DT5432

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693334, 725574

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Highest Expressing Human Cell Lines

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malfunction

Methanococcus maripaludis

Q6LZB6; Q6LZB5, Q6M0F5; Q6M0F6

Methanococcus maripaludis has two IOR homologs. A deletion mutant for one of these homologs contains 76, 74, and 42% lower activity for phenylpyruvate, p-hydroxyphenylpyruvate, and indolepyruvate oxidation, respectively, than the wild type. Growth of this mutant in minimal medium is inhibited by the aryl acids, but the aromatic amino aciuds partially restore growth

727742

155000

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sedimentation equilibrium and sedimentation velocity experiments

170000

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gel filtration

180000

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gel filtration

192000

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gel filtration

21000

23000

24000

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2 * 71000 + 2 * 24000, alpha2,beta2, SDS-PAGE

639362, 644703

66000

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2 * 66000 + 2 * 23000, alpha2,beta2, SDS-PAGE

67000

71000

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2 * 71000 + 2 * 24000, alpha2,beta2, SDS-PAGE

heterotetramer

tetramer

8 - 10

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not active at pH 5.2 and pH 11.0

644700

100

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half-life 62 min

105

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half-life 20 min

60 - 110

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a slight decrease in activity is observed below 90°C for at least 4 h. The enzyme exhibits a half-life of 62 min at 100°C, 40 min at 103°C, 20 min at 105°C, 5 min at 108°C, and less than 5 min at 110°C

80

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virtually inactive at 25°C, quite thermostable, with a half-life of activity at 80°C of about 80 min under anaerobic conditions

during a long complicated purification process, the enzyme loses much activity

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25°C, aerobic conditions, half-life 7 h

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725574

enzyme is sensitive to inactivation by O2, losing 50% of its activity after exposure to air for 20 min at 23°C

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644700

half-life in presence of air is 15 min at 25°C

O07835; O07836

644701

irreversibly inactivated by oxygen

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639362

the enzyme is oxygen-sensitive with a half-life of 7 h at 25°C under aerobic conditions

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725574

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by affinity chromatography, 74fold

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purification under extremely anaerobic conditions in presence of 2mM dithiothreitol and 2mM sodium dithionite to protect against oxygen attack, and also 1mM MgSO4,1mM thiamine diphosphate and 0.2M NaCl, additives which have been found to stabilize

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under extremely anaerobic conditions with all buffers containing 2 mM dithiothreitol and 2 mM dithiothreitol. Q Sepharose column chromatography, hydroxyapatite column chromatography, Blue Sepharose column chromatography, and Superdex 200 gel filtration

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-

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639362

gene cloning and sequence analysis of the IOR gene, 2 genes iorA and iorB, encoding alpha and beta subunits are tandemly arranged, KOD1-IOR overproduced in anaerobically incubated Escherichia coli BL21(DE3)

activity decreases significantly when the organism is grown on maltose plus S(0)

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analysis

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development of an effective affinity chromatography technique