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Literature summary 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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.204 [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
-
?
2.3.1.204 [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

EC Number Organism UniProt Comment Textmining
2.3.1.204 Bacillus subtilis
-
-
-
2.3.1.204 Bacillus subtilis JH642
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-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.204 [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
-
?
2.3.1.204 [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
-
?
2.3.1.204 [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
-
?
2.3.1.204 [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

EC Number Synonyms Comment Organism
2.3.1.204 LIPL
-
Bacillus subtilis

General Information

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