EC Number |
Natural Substrates |
---|
2.3.1.181 | an octanoyl-[acyl-carrier protein] + a protein |
- |
2.3.1.181 | an octanoyl-[acyl-carrier protein] + a protein |
LipM specifically modifies the glycine cleavage system protein, GcvH |
2.3.1.181 | an octanoyl-[acyl-carrier protein] + glycine cleavage system protein |
- |
2.3.1.181 | octanoyl-[acyl-carrier protein] + a protein |
- |
2.3.1.181 | octanoyl-[acyl-carrier protein] + a protein |
LipB (EC 2.3.11.181) is responsible for octanoylation of the E2 components of 2-oxoacid dehydrogenases to provide the substrates of LipA (EC 2.7.7.63), an S-adenosyl-L-methionine radical enzyme that inserts two sulfur atoms into the octanoyl moiety to give the active lipoylated dehydrogenase complexes. LipB accumulates an octanoyl-enzyme intermediate with no sign of a lipoyl-enzyme intermediate |
2.3.1.181 | octanoyl-[acyl-carrier protein] + apo-H protein |
LipB reaction represents the first committed step in the biosynthesis of the lipoyl cofactor. apo-H protein is the lipoyl bearing subunit of the glycine cleavage system |
2.3.1.181 | octanoyl-[acyl-carrier protein] + protein |
- |
2.3.1.181 | octanoyl-[acyl-carrier protein] + protein |
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of glycine cleavage system (H protein) |
2.3.1.181 | octanoyl-[acyl-carrier protein] + protein |
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain) |
2.3.1.181 | octanoyl-[acyl-carrier protein] + protein |
first committed step in the biosynthesis of lipoyl cofactor. The lipoyl cofactor is essential for the function of pyruvate dehydrogenase (E2 domain) and of the 2-oxoglutarate dehydrogenase complex |