In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the
amidotransfer of the octanoyl moiety from [glycine cleavage system H]-N6-octanoyl-L-lysine (i.e. octanoyl-GcvH) to the E2 subunit (dihydrolipoamide acetyltransferase) of pyruvate dehydrogenase.
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The enzyme appears in viruses and cellular organisms
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] = glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine
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SYSTEMATIC NAME
IUBMB Comments
[glycine cleavage system H]-N6-octanoyl-L-lysine:[lipoyl-carrier protein]-N6-L-lysine octanoyltransferase
In the bacterium Bacillus subtilis it has been shown that the enzyme catalyses the
amidotransfer of the octanoyl moiety from [glycine cleavage system H]-N6-octanoyl-L-lysine (i.e. octanoyl-GcvH) to the E2 subunit (dihydrolipoamide acetyltransferase) of pyruvate dehydrogenase.
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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History
Enzyme Nomenclature
2.3.1.204 octanoyl-[GcvH]:protein N-octanoyltransferase
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