EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.8.1.8 | biotin-PEG-Glu-Ser-Val-([8,8,8-2H3]-N6-octanoyl)Lys-Ala-Ala-Ser-As + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [4Fe-4S] ferredoxin |
- |
Thermus thermophilus |
biotin-PEG-Glu-Ser-Val-([8,8,8-2H3]-N6-lipoyl)Lys-Ala-Ala-Ser-As + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [4Fe-4S] ferredoxin |
- |
? |
2.8.1.8 | biotin-PEG-Glu-Ser-Val-([8,8,8-2H3]-N6-octanoyl)Lys-Ala-Ala-Ser-As + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [4Fe-4S] ferredoxin |
- |
Escherichia coli |
biotin-PEG-Glu-Ser-Val-([8,8,8-2H3]-N6-lipoyl)Lys-Ala-Ala-Ser-As + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [4Fe-4S] ferredoxin |
- |
? |
2.8.1.8 | Glu-Ser-Val-(N6-octanoyl)Lys-Ala-Ala-Ser-Asp + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [4Fe-4S] dithionite |
- |
Thermus thermophilus |
Glu-Ser-Val-(N6-lipoyl)Lys-Ala-Ala-Ser-Asp + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [4Fe-4S] dithionite |
- |
? |
2.8.1.8 | Glu-Ser-Val-(N6-octanoyl)Lys-Ala-Ala-Ser-Asp + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [4Fe-4S] dithionite |
- |
Escherichia coli |
Glu-Ser-Val-(N6-lipoyl)Lys-Ala-Ala-Ser-Asp + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [4Fe-4S] dithionite |
- |
? |
2.8.1.8 | H protein N6-(octanoyl)lysine + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] dithionite |
- |
Mycobacterium tuberculosis |
H protein N6-(lipoyl)lysine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] dithionite |
- |
? |
2.8.1.8 | H protein N6-(octanoyl)lysine + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced [2Fe-2S] flavodoxin |
- |
Mycobacterium tuberculosis |
H protein N6-(lipoyl)lysine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized [2Fe-2S] flavodoxin |
- |
? |
2.8.1.8 | more |
final step in de novo biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain) |
Escherichia coli |
? |
- |
? |
2.8.1.8 | more |
final step in de novo biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain) |
Neurospora crassa |
? |
- |
? |
2.8.1.8 | more |
final step in de novo biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain) |
Pisum sativum |
? |
- |
? |
2.8.1.8 | more |
insertion of sulfur into octanoyl groups is first at C6 to form an enzyme bound intermediate, and in a subsequent step a second sulfur is inserted at C8 |
Saccharolobus solfataricus |
? |
- |
? |