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Literature summary for 3.5.1.18 extracted from
- The dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase from Haemophilus influenzae contains two active-site histidine residues (2009), J. Biol. Inorg. Chem., 14, 1-10.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene dapE, expression of wild-type enzyme and mutants in Escherichia coli BL21, subcloning in Escherichia coli JM109 | Haemophilus influenzae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H349A | site-directed mutagenesis, inactive mutant | Haemophilus influenzae |
| H67A | site-directed mutagenesis, the mutant shows 180fold decreased activity compred to the wild-type enzyme. Approximately 70% of the maximal catalytic activity is recovered after the addition of 1 equiv of Zn2+ | Haemophilus influenzae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.73 | - |
N-succinyl-LL-2,6-diaminopimelic acid | pH 7.5, 30°C, wild-type enzyme | Haemophilus influenzae |  |
| 1.4 | - |
N-succinyl-LL-2,6-diaminopimelic acid | pH 7.5, 30°C, mutant H67A | Haemophilus influenzae | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | can substitute for Zn2+ | Haemophilus influenzae | |
| Zn2+ | modelling of binding structure, overview | Haemophilus influenzae | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haemophilus influenzae | - |
gene dapE | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type enzyme and mutants from Escherichia coli BL21 | Haemophilus influenzae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| N-succinyl-LL-2,6-diaminopimelic acid + H2O | - |
Haemophilus influenzae | succinate + LL-2,6-diaminoheptanedioate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | three-dimensional homology structure of the DapE, based on the crystal structure of the DapE from Neisseria meningitidis as template and and superimposed on the structure of the aminopeptidase from Aeromonas proteolytica, overview | Haemophilus influenzae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DapE | - |
Haemophilus influenzae |
| N-succinyl-L,L-diaminopimelic acid desuccinylase | - |
Haemophilus influenzae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Haemophilus influenzae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.5 | - |
N-succinyl-LL-2,6-diaminopimelic acid | pH 7.5, 30°C, mutant H67A | Haemophilus influenzae | |
| 140 | - |
N-succinyl-LL-2,6-diaminopimelic acid | pH 7.5, 30°C, wild-type enzyme | Haemophilus influenzae | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Haemophilus influenzae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | DapE is involved in the meso-diaminopimelate (mDAP)/lysine biosynthetic pathway | Haemophilus influenzae |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.1 | - |
N-succinyl-LL-2,6-diaminopimelic acid | pH 7.5, 30°C, mutant H67A | Haemophilus influenzae | |
| 204 | - |
N-succinyl-LL-2,6-diaminopimelic acid | pH 7.5, 30°C, wild-type enzyme | Haemophilus influenzae | |
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