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
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3.5.1.18
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haemophilus
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l-captopril
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peptidoglycan
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meso-diaminopimelic
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acetylornithine
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metallohydrolase
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drug development
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medicine
- 3.5.1.18
- haemophilus
- l-captopril
- peptidoglycan
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meso-diaminopimelic
- acetylornithine
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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
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General Information
General Information on EC 3.5.1.18 - succinyl-diaminopimelate desuccinylase
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evolution
malfunction
metabolism
physiological function
additional information
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the enzyme is composed of catalytic and dimerization domains, and belongs to the M20 peptidase family
evolution
the enzyme is composed of catalytic and dimerization domains, and belongs to the M20 peptidase family
deletion of the DapE gene is lethal to Helicobacter pylori, since the organism has no alternative pathway for lysine biosynthesis
malfunction
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deletion of the DapE gene is lethal to Helicobacter pylori, since the organism has no alternative pathway for lysine biosynthesis
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DapE is involved in the meso-diaminopimelate (mDAP)/lysine biosynthetic pathway
metabolism
DapE is involved in the meso-diaminopimelate, mDAP/lysine biosynthetic pathway
metabolism
the enzyme catalyzes the seventh reaction step of the succinyl pathway
metabolism
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the enzyme is part of the lysine biosynthetic pathway which is indispensable for bacterial survival
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DapE is a critical bacterial enzyme for the construction of the bacterial cell wall.
physiological function
DapE is essential for cell growth and proliferation
physiological function
critical enzyme of the lysine biosynthetic pathway
physiological function
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the enzyme is a constituent of the divisome through association with the Ter complex. The enzyme facilitates functional Z ring formation by strengthening the Ter signal via ZapB. DapE depends on ZapB to localize to the Z ring. DapE shows a strong interaction with ZapB and requires the presence of ZapB to exert its function in division
physiological function
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critical enzyme of the lysine biosynthetic pathway
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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
additional information
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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
additional information
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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
additional information
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
additional information
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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