EC Number |
Inhibitors |
Structure |
---|
2.3.1.191 | (3R)-3-hydroxymyristoyl-[acyl-carrier protein] |
- |
|
2.3.1.191 | 4-(2-chlorophenyl)-3-hydroxy-7,7-dimethyl-2-phenyl-7,8-dihydro-2H-pyrazolo[3,4-b]quinolin-5(6H)-one |
- |
|
2.3.1.191 | Mg2+ |
- |
|
2.3.1.191 | acyl-carrier protein |
competitive inhibitor with respect to (3R)-3-hydroxymyristoyl-[acyl-carrier protein] and a noncompetitive inhibitor with respect to UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine |
|
2.3.1.191 | (3R)-3-hydroxylauroyl-methylphosphopantetheine |
competitive inhibitor with respect to UDP-3-O-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine and an uncompetitive inhibitor with respect to (3R)-3-hydroxymyristoyl-[acyl-carrier protein] |
|
2.3.1.191 | more |
divalent cations inhibit (3R)-3-hydroxymyristoyl-[acyl-carrier protein]-dependent acylation but not (3R)-3-hydroxylauroylmethylphosphopantetheine-dependent acylation, indicating that the acidic recognition helix of (3R)-3-hydroxymyristoyl-[acyl-carrier protein] contributes to binding; Na+ and K+ ions do not inhibit LpxD activity |
|
2.3.1.191 | TNLYMLPKWDIP-NH2 |
i.e. peptide RJPXD33 |
|
2.3.1.191 | RJPXD33 |
i.e. TNLYMLPKWDIP, peptide inhibitor, binds to both UDP-N-acetylglucosamine acyltransferase (LpxA, EC 2.3.1.129) and UDP-3-O-(acyl)-glucosamine acyltransferase. Comparison with binding to LpxA suggests overlap with the acyl-phosphopantetheine arm of acyl-ACP, thereby inhibiting acyl-ACP from binding to LpxD. RJPXD33 binds to LpxD without the prior binding of other ligands |
|
2.3.1.191 | Ca2+ |
inhibition is overcome by the addition of excess (3R)-3-hydroxymyristoyl-[acyl-carrier protein] |
|
2.3.1.191 | UDP-2-N-((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine |
noncompetitive inhibitor against both substrates |
|