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Literature summary for 2.3.1.204 extracted from

  • Rasetto, N.B.; Lavatelli, A.; Martin, N.; Mansilla, M.C.
    Unravelling the lipoyl-relay of exogenous lipoate utilization in Bacillus subtilis (2019), Mol. Microbiol., 112, 302-316 .
    View publication on PubMed
Search for more literature for 2.3.1.204

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] Bacillus subtilis the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
 ?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] Bacillus subtilis JH642 the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis JH642
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
-
 Bacillus subtilis glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
 ?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging Bacillus subtilis glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
 ?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
-
 Bacillus subtilis JH642 glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
 ?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging Bacillus subtilis JH642 glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
-
 ?

Synonyms

Synonyms Comment Organism
LIPL
-
 Bacillus subtilis

General Information

General Information Comment Organism
metabolism the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging Bacillus subtilis