Literature summary extracted from
Nocek, B.P.; Gillner, D.M.; Fan, Y.; Holz, R.C.; Joachimiak, A.
Structural basis for catalysis by the mono- and dimetalated forms of the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (2010), J. Mol. Biol., 397, 617-626.
Application
EC Number |
Application |
Comment |
Organism |
---|
3.5.1.18 |
drug development |
development of antimicrobial agents that target DapE |
Haemophilus influenzae |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.5.1.18 |
ultrapure recombinant DapE with one and two zinc ions bound in the active site, respectively, at 16°C, by vapor diffusion in hanging drops containing 1 ml of precipitant solution containing 1 M ammonium sulfate, 0.2 M NaCl, and 0.1 M Na acetate, pH 4.4, and 0.001 ml of 13 mg/ml of DapE with three equivalents of zinc, 2 weeks, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution |
Haemophilus influenzae |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.5.1.18 |
additional information |
design of structure-based, catalytic inhibitors, overview |
Haemophilus influenzae |
|
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
3.5.1.18 |
730 |
- |
N-succinyl LL-diaminopimelic acid |
pH not specified in the publication, temperature not specified in the publication |
Haemophilus influenzae |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
3.5.1.18 |
sulfate |
in one of the monomers of the ZnZn_DapE structure, both of these residues form a charged dipole interaction with a sulfate ion, a possible mimic of the carboxylic group of the substrate |
Haemophilus influenzae |
|
3.5.1.18 |
Zn2+ |
required for activity, DapE has one or two zinc ions bound in the active site, the two forms show different activity, structures of monometalated and dimetalated forms, overview |
Haemophilus influenzae |
|
Molecular Weight [Da]
EC Number |
Molecular Weight [Da] |
Molecular Weight Maximum [Da] |
Comment |
Organism |
---|
3.5.1.18 |
41500 |
- |
2 * 41500, SDS-PAGE |
Haemophilus influenzae |
3.5.1.18 |
83000 |
- |
about |
Haemophilus influenzae |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
3.5.1.18 |
N-succinyl LL-diaminopimelic acid + H2O |
Haemophilus influenzae |
- |
succinate + LL-2,6-diaminoheptanedioate |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.5.1.18 |
Haemophilus influenzae |
P44514 |
gene dapE |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
3.5.1.18 |
N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate |
structure-activity relationship and catalytic mechanism of peptide bond cleavage by DapE enzymes, overview. The catalytic domain is composed of residues 1-179 and 293-376 |
Haemophilus influenzae |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.5.1.18 |
N-succinyl LL-diaminopimelic acid + H2O |
- |
Haemophilus influenzae |
succinate + LL-2,6-diaminoheptanedioate |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
3.5.1.18 |
dimer |
2 * 41500, SDS-PAGE |
Haemophilus influenzae |
3.5.1.18 |
More |
the core of the catalytic domain consists of an eight-stranded twisted beta-sheet that is sandwiched between seven alpha-helices, active site structure and structure-activity relationship, overview |
Haemophilus influenzae |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.5.1.18 |
DapE |
- |
Haemophilus influenzae |
3.5.1.18 |
N-succinyl-L,L-diaminopimelic acid desuccinylase |
- |
Haemophilus influenzae |
Turnover Number [1/s]
EC Number |
Turnover Number Minimum [1/s] |
Turnover Number Maximum [1/s] |
Substrate |
Comment |
Organism |
Structure |
---|
3.5.1.18 |
140 |
- |
N-succinyl LL-diaminopimelic acid |
pH not specified in the publication, temperature not specified in the publication |
Haemophilus influenzae |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.5.1.18 |
metabolism |
DapE is involved in the meso-diaminopimelate, mDAP/lysine biosynthetic pathway |
Haemophilus influenzae |
3.5.1.18 |
physiological function |
DapE is essential for cell growth and proliferation |
Haemophilus influenzae |