EC Number   |
General Information |
Reference |
|---|
    3.5.1.18 | evolution |
the enzyme is composed of catalytic and dimerization domains, and belongs to the M20 peptidase family |
735140 |
| 3.5.1.18 | malfunction |
deletion of the DapE gene is lethal to Helicobacter pylori, since the organism has no alternative pathway for lysine biosynthesis |
-, 754194 |
| 3.5.1.18 | metabolism |
DapE is involved in the meso-diaminopimelate (mDAP)/lysine biosynthetic pathway |
712506 |
| 3.5.1.18 | metabolism |
DapE is involved in the meso-diaminopimelate, mDAP/lysine biosynthetic pathway |
712756 |
| 3.5.1.18 | metabolism |
the enzyme catalyzes the seventh reaction step of the succinyl pathway |
733015 |
| 3.5.1.18 | metabolism |
the enzyme is part of the lysine biosynthetic pathway which is indispensable for bacterial survival |
734849 |
| 3.5.1.18 | more |
DapE residues H355 and H80 are active site ligands, divalent metal binding properties of co-catalytic metallohydrolase active site, overview. Three-dimensional homological structure molecular modeling of N-acetyl-L-ornithine deacetylase, EC 3.5.1.16, from Escherichia coli, using the X-ray crystal structure of the DapE from Haemophilus influenzae, PDB ID 3IC1, as template |
735279 |
| 3.5.1.18 | more |
residues Arg178, Thr325, and Asn345 play a role in substrate identification and stabilization of the enzyme active site. The glycine rich loop, Gly322-Ser326, facilitates tight binding of the substrate in the enzyme active site. Computational structure modeling by quantum mechanics/molecular mechanics calculations using the enzyme crystal structure PDB ID 3IC1 |
734849 |
| 3.5.1.18 | more |
structural comparisons of wild-type and inactive monomeric DapE enzymes with other M20 peptidases, active site and zinc binding structure, molecular modeling and dynamics simulations, overview. The dimerization domain in DapE enzymes is required for catalysis. Removal of the dimerization domain increases the flexibility of a conserved active site loop that may provide critical interactions with the substrate |
735140 |
| 3.5.1.18 | physiological function |
critical enzyme of the lysine biosynthetic pathway |
-, 754194 |
