In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the amidotransfer of the dihydrolipoyl moiety from either the H protein of the glycine cleavage system (EC 1.4.1.27) or the E2 component (dihydrolipoamide acetyltransferase) of the 2-oxoglutarate dehydrogenase system (EC 1.2.1.105) to the E2 component of other 2-oxoacid dehydrogenase systems: the pyruvate dehydrogenase system (EC 1.2.1.104), the branched-chain α-keto acid dehydrogenase system (EC 1.2.1.25), and the acetoin dehydrogenase system (EC 2.3.1.190).
The enzyme appears in viruses and cellular organisms
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[glycine cleavage system H protein]-N6-dihydrolipoyl-L-lysine + a [lipoyl-carrier protein] = [glycine cleavage system H protein] + a [lipoyl-carrier protein]-N6-dihydrolipoyl-L-lysine
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SYSTEMATIC NAME
IUBMB Comments
[glycine cleavage system H protein]-N6-dihydrolipoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine dihydrolipoyltransferase
In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the amidotransfer of the dihydrolipoyl moiety from either the H protein of the glycine cleavage system (EC 1.4.1.27) or the E2 component (dihydrolipoamide acetyltransferase) of the 2-oxoglutarate dehydrogenase system (EC 1.2.1.105) to the E2 component of other 2-oxoacid dehydrogenase systems: the pyruvate dehydrogenase system (EC 1.2.1.104), the branched-chain alpha-keto acid dehydrogenase system (EC 1.2.1.25), and the acetoin dehydrogenase system (EC 2.3.1.190).
Substrates: the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging Products: -
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[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
Substrates: the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging Products: -
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
Substrates: the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging Products: -
?
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein]
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
Substrates: the enzyme LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging Products: -
the enzyme is required for lipoylation of the E2 subunits of pyruvate dehydrogenase and branched-chain 2-oxoacid dehydrogenase complexes. LipL facilitates lipoyl relay between E2 subunits and between H proteins, a property that potentially constitutes an adaptive response to nutrient scarcity in the host, as LipL is required for virulence during infection. LipL is involved in facilitating flexible lipoyl relay between proteins
the enzyme is required for lipoylation of the E2 subunits of pyruvate dehydrogenase and branched-chain 2-oxoacid dehydrogenase complexes. LipL facilitates lipoyl relay between E2 subunits and between H proteins, a property that potentially constitutes an adaptive response to nutrient scarcity in the host, as LipL is required for virulence during infection. LipL is involved in facilitating flexible lipoyl relay between proteins
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