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
-
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
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Subunits
Subunits on EC 3.5.1.18 - succinyl-diaminopimelate desuccinylase
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dimer
homodimer
monomer
additional information
dimer
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the DapE enzyme exists in a dimeric form with each monomer consisting of a catalytic and dimerization domain
dimer
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the enzyme is composed of catalytic and dimerization domains, the dimerization domain in DapE enzymes is required for catalysis
dimer
the enzyme is composed of catalytic and dimerization domains, the dimerization domain in DapE enzymes is required for catalysis
the core of the catalytic domain consists of an eight-stranded twisted beta-sheet that is sandwiched between seven alpha-helices, active site structure and structure-activity relationship, overview
additional information
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the core of the catalytic domain consists of an eight-stranded twisted beta-sheet that is sandwiched between seven alpha-helices, active site structure and structure-activity relationship, overview
additional information
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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