3.5.1.18: succinyl-diaminopimelate desuccinylase
This is an abbreviated version!
For detailed information about succinyl-diaminopimelate desuccinylase, go to the full flat file.
Word Map on EC 3.5.1.18
-
3.5.1.18
-
haemophilus
-
l-captopril
-
peptidoglycan
-
meso-diaminopimelic
-
acetylornithine
-
metallohydrolase
-
drug development
-
medicine
- 3.5.1.18
- haemophilus
- l-captopril
- peptidoglycan
-
meso-diaminopimelic
- acetylornithine
-
metallohydrolase
- drug development
- medicine
Reaction
Synonyms
Cgl1109, DapE, dapE-encoded N-succinyl-LL-diaminopimelic acid desuccinylase, HiDapE, N-succinyl-L,L-diaminopimelic acid desuccinylase, N-succinyl-L-alpha,epsilon-diaminopimelic acid deacylase, Rv1202, S-DAP deacylase, SDAP, sDap desuccinylase, succinyl-diaminopimelate desuccinylase, succinyldiaminopimelate desuccinylase
ECTree
Advanced search results
Metals Ions
Metals Ions on EC 3.5.1.18 - succinyl-diaminopimelate desuccinylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Co2+
Mn2+
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
Zn2+
Co2+
-
metal-dependent enzyme (Zn2+ or Co2+). Determination of metal stoichiometry by ICP-AES indicates one tightly bound metal ion, while sequence homologies suggest the presence of two metal binding sites
Co2+
EPR and MCD data indicate that the two Co(II) ions in DapE are antiferromagnetically coupled
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
Zn2+
-
the enzyme requires two Zn2+ ions. Each of the Zn(II) ions adopts a distorted tetrahedral geometry and is coordinated by one imidazole group, H67 for Zn1 and H349 for Zn2, and one carboxylate group, E163 for Zn1 and E135 for Zn2. Both Zn(II) ions are bridged by an additional carboxylate groups of residue D100 on one side and water/hydroxide on the opposite side, forming a (mu-aquo)(mu-carboxylato)dizinc(II) core with one terminal carboxylate and one histidine residue at each metal site
Zn2+
-
di-nuclear Zn2+ enzyme, the side chain of Asp100 bridges the two Zn centers of the enzyme
Zn2+
-
required, dinuclear Zn(II)-loaded enzyme, binding structure, overview
Zn2+
-
required, the enzyme binds two Zn(II) ions in non-interactive binding sites with Kd values for the first Zn(II) binding event of 0.0044 mM, whereas the observed Kd values for the second metal binding event in DapE is 0.0136 mM
Zn2+
-
metal-dependent enzyme (Zn2+ or Co2+). Determination of metal stoichiometry by ICP-AES indicates one tightly bound metal ion, while sequence homologies suggest the presence of two metal binding sites
Zn2+
two Zn metal centers are essential to the catalytic action of the DapE enzyme. His67, His349, and Glu134 residues in the active site
Zn2+
untreated enzyme contains 0.8 Zn2+ per monomer and was enzymatically active
Zn2+
-
the enzyme possesses a catalytic domain with a di-zinc active site
Zn2+
required, dinuclear Zn(II)-loaded enzyme, binding structure, overview