EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
2.3.1.181 | LipL | is essential for lipoic acid synthesis, but has no detectable octanoyltransferase or ligase activity either in vitro or in vivo. It catalyses the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the E2 subunit of pyruvate dehydrogenase | Bacillus subtilis |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.3.1.200 | expressed in Escherichia coli strain QC143 | Bacillus subtilis |
2.3.1.204 | expressed in Escherichia coli | Bacillus subtilis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.3.1.200 | C150A | the mutation results in loss of enzymatic activity and the inability to form an acyl-enzyme intermediate | Bacillus subtilis |
2.3.1.200 | C150S | the mutation results in loss of enzymatic activity and the inability to form an acyl-enzyme intermediate | Bacillus subtilis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.3.1.204 | 31420 | - |
calculated from amino acid sequence | Bacillus subtilis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.3.1.181 | an octanoyl-[acyl-carrier protein] + a protein | Bacillus subtilis | LipM specifically modifies the glycine cleavage system protein, GcvH | a 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] | - |
? | |
2.3.1.204 | [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 | - |
r | |
2.3.1.204 | [glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] | Bacillus subtilis 168 | - |
glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.3.1.181 | Bacillus subtilis | - |
gene lipM | - |
2.3.1.200 | Bacillus subtilis | - |
- |
- |
2.3.1.204 | Bacillus subtilis | P39648 | - |
- |
2.3.1.204 | Bacillus subtilis 168 | P39648 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.3.1.200 | Ni-NTA resin column chromatography | Bacillus subtilis |
2.3.1.204 | - |
Bacillus subtilis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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] + glycine cleavage system protein | - |
Bacillus subtilis | glycine cleavage system protein-N6-(octanoyl)lysine + an [acyl-carrier protein] | - |
? | |
2.3.1.200 | octanoyl-glycine cleavage system H protein + pyruvate dehydrogenase subunit E2 | - |
Bacillus subtilis | glycine cleavage system H protein + pyruvate dehydrogenase subunit E2-octanoyl | - |
r | |
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 | - |
r | |
2.3.1.204 | [glycine cleavage system H]-N6-octanoyl-L-lysine + a [lipoyl-carrier protein] | - |
Bacillus subtilis 168 | glycine cleavage system H + a [lipoyl-carrier protein]-N6-octanoyl-L-lysine | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.3.1.181 | ACP: GcvH octanoyltransferase | - |
Bacillus subtilis |
2.3.1.181 | LipM | - |
Bacillus subtilis |
2.3.1.200 | GcvH:E2 amidotransferase | - |
Bacillus subtilis |
2.3.1.200 | GcvH:[lipoyl domain] amidotransferase | - |
Bacillus subtilis |
2.3.1.200 | LIPL | - |
Bacillus subtilis |
2.3.1.200 | ywfL | - |
Bacillus subtilis |
2.3.1.204 | LIPL | - |
Bacillus subtilis |
2.3.1.204 | octanoyl-[GcvH]:E2 amidotransferase | - |
Bacillus subtilis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.3.1.181 | evolution | LipM and LipL phylogenetic tree analysis, overview | Bacillus subtilis |
2.3.1.181 | physiological function | LipM specifically modifies the glycine cleavage system protein, GcvH. GcvH is required in Bacillus subtilis lipoic acid biosynthesis, overview. LipM is an octanoyltransferase required for lipoic acid synthesis, and LipL is essential for lipoic acid synthesis, but has no detectable octanoyltransferase or ligase activity either in vitro or in vivo, it catalyses the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-glycine cleavage system protein to the E2 subunit of pyruvate dehydrogenase | Bacillus subtilis |
2.3.1.200 | metabolism | the enzyme is essential for lipoic acid synthesis, but has no detectable octanoyltransferase or ligase activity either in vitro or in vivo. The enzyme is required for PdhC modification | Bacillus subtilis |