EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.3.1.181 | an octanoyl-[acyl-carrier protein] + a protein |
- |
Bacillus subtilis |
a protein N6-(octanoyl)lysine + an [acyl-carrier protein] |
- |
? |
2.3.1.181 | an octanoyl-[acyl-carrier protein] + a protein |
LipM specifically modifies the glycine cleavage system protein, GcvH |
Bacillus subtilis |
a protein N6-(octanoyl)lysine + an [acyl-carrier protein] |
- |
? |
2.3.1.181 | an octanoyl-[acyl-carrier protein] + a protein |
acyl-enzyme intermediate mechanism |
Bacillus subtilis |
a protein N6-(octanoyl)lysine + an [acyl-carrier protein] |
- |
? |
2.3.1.181 | an octanoyl-[acyl-carrier protein] + GCSH protein |
- |
Mus musculus |
GCSH protein N6-(octanoyl)lysine + an [acyl-carrier protein] |
- |
? |
2.3.1.181 | an octanoyl-[acyl-carrier protein] + glycine cleavage system protein |
- |
Bacillus subtilis |
glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein] |
- |
? |
2.3.1.181 | lipoyl-[acyl-carrier protein] + apo-pyruvate dehydrogenase protein |
- |
Escherichia coli |
? |
- |
? |
2.3.1.181 | more |
Lip3 is unable to modify either lipoyl domains or glycine cleavage system 3 when provided with free octanoate, ATP and MgCl2 |
Saccharomyces cerevisiae |
? |
- |
? |
2.3.1.181 | more |
pyruvate dehydrogenase E2 domain is exclusively octanoylated by lipoate-protein ligase LPLA, EC 2.7.7.63 |
Arabidopsis thaliana |
? |
- |
? |
2.3.1.181 | octanoyl-CoA + [glycine cleavage system 3]-L-lysine |
- |
Saccharomyces cerevisiae |
[glycine cleavage system 3]-N6-octanoyl-L-lysine + CoA |
- |
? |
2.3.1.181 | octanoyl-CoA + [oxoglutarate dehydrogenase]-L-lysine |
- |
Saccharomyces cerevisiae |
[oxoglutarate dehydrogenase]-N6-octanoyl-L-lysine + CoA |
- |
? |