Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Gillner, D.; Bienvenue, D.; Nocek, B.; Joachimiak, A.; Zachary, V.; Bennett, B.; Holz, R.
    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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.18 gene dapE, expression of wild-type enzyme and mutants in Escherichia coli BL21, subcloning in Escherichia coli JM109 Haemophilus influenzae

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.18 H349A site-directed mutagenesis, inactive mutant Haemophilus influenzae
3.5.1.18 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.18 0.73
-
 N-succinyl-LL-2,6-diaminopimelic acid pH 7.5, 30°C, wild-type enzyme Haemophilus influenzae
3.5.1.18 1.4
-
 N-succinyl-LL-2,6-diaminopimelic acid pH 7.5, 30°C, mutant H67A Haemophilus influenzae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.18 Co2+ can substitute for Zn2+ Haemophilus influenzae
3.5.1.18 Zn2+ modelling of binding structure, overview Haemophilus influenzae

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.18 Haemophilus influenzae
-
 gene dapE
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.18 recombinant wild-type enzyme and mutants from Escherichia coli BL21 Haemophilus influenzae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.18 N-succinyl-LL-2,6-diaminopimelic acid + H2O
-
 Haemophilus influenzae succinate + LL-2,6-diaminoheptanedioate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.18 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.18 30
-
 assay at 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 1.5
-
 N-succinyl-LL-2,6-diaminopimelic acid pH 7.5, 30°C, mutant H67A Haemophilus influenzae
3.5.1.18 140
-
 N-succinyl-LL-2,6-diaminopimelic acid pH 7.5, 30°C, wild-type enzyme Haemophilus influenzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.18 7.5
-
 assay at 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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.1.18 1.1
-
 N-succinyl-LL-2,6-diaminopimelic acid pH 7.5, 30°C, mutant H67A Haemophilus influenzae
3.5.1.18 204
-
 N-succinyl-LL-2,6-diaminopimelic acid pH 7.5, 30°C, wild-type enzyme Haemophilus influenzae