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Literature summary for 2.8.1.8 extracted from

  • Jin, J.Q.; Hachisuka, S.I.; Sato, T.; Fujiwara, T.; Atomi, H.
    A structurally novel lipoyl synthase in the hyperthermophilic archaeon Thermococcus kodakarensis (2020), Appl. Environ. Microbiol., 86, e01359 .
    View publication on PubMed
Search for more literature for 2.8.1.8

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermococcus kodakarensis

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis Q5JEV3
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-
Thermococcus kodakarensis Q5JHS9
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Thermococcus kodakarensis ATCC BAA-918 Q5JEV3
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Thermococcus kodakarensis ATCC BAA-918 Q5JHS9
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[protein]-N6-(octanoyl)-L-lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ substrate is a chemically synthesized octanoyl-octapeptide whose sequence corresponds to that of the lipoyl domain in the H-protein of Thermococcus kodakarensis Thermococcus kodakarensis [protein]-N6-[(R)-dihydrolipoyl]-L-lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [2Fe-2S] ferredoxin
-
 ?
[protein]-N6-(octanoyl)-L-lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 2 oxidized [2Fe-2S] ferredoxin + 6 H+ substrate is a chemically synthesized octanoyl-octapeptide whose sequence corresponds to that of the lipoyl domain in the H-protein of Thermococcus kodakarensis Thermococcus kodakarensis ATCC BAA-918 [protein]-N6-[(R)-dihydrolipoyl]-L-lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 2 reduced [2Fe-2S] ferredoxin
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 ?

Synonyms

Synonyms Comment Organism
LipS1
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 Thermococcus kodakarensis
LipS2
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 Thermococcus kodakarensis
TK2109
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 Thermococcus kodakarensis
TK2248
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 Thermococcus kodakarensis

Cofactor

Cofactor Comment Organism Structure
[4Fe-4S]-center
-
 Thermococcus kodakarensis

General Information

General Information Comment Organism
physiological function a gene disruption mutant and a genes TK2109/TK2248 disruption mutant are not able to grow in a synthetic medium without Ser and lipoic acid. In the absence of biotin, the TK2109/TK2248 double mutant strain displays growth through six serial cultures as in the case of host strain Thermococcus kodakarensis
physiological function a gene disruption mutant and a genes TK2109/Tkk248 disruption mutant are not able to grow in a synthetic medium without Ser and lipoic acid. In the absence of biotin, the TK2109/TK2248 double mutant strain displays growth through six serial cultures as in the case of host strain Thermococcus kodakarensis