5.1.1.7: diaminopimelate epimerase
This is an abbreviated version!
For detailed information about diaminopimelate epimerase, go to the full flat file.
Word Map on EC 5.1.1.7
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5.1.1.7
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meso-dap
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racemase
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peptidoglycan
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l-lysine
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drug development
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ll-dap
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plp-independent
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meso-diaminopimelate
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epimerization
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d-cycloserine
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stereoinversion
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l,l-diaminopimelate
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two-base
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analysis
- 5.1.1.7
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meso-dap
- racemase
- peptidoglycan
- l-lysine
- drug development
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ll-dap
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plp-independent
- meso-diaminopimelate
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epimerization
- d-cycloserine
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stereoinversion
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l,l-diaminopimelate
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two-base
- analysis
Reaction
Synonyms
CgDapF, DAP, DAP epimerase, DAP-epimerase, DapF, DapFCT, diaminopimelate epimerase, Diaminopimelic acid epimerase, Diaminopimelic epimerase, Epimerase, diaminopimelate, LL-Diaminopimelate epimerase, MtDapF, YddE
ECTree
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General Information
General Information on EC 5.1.1.7 - diaminopimelate epimerase
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evolution
metabolism
physiological function
additional information
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the enzyme is a member of the pyridoxal 5'-phosphate-independent racemase family of enzymes
evolution
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the enzyme is a member of the pyridoxal 5'-phosphate-independent racemase family of enzymes
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meso-diaminopimelate is a biosynthetic precursor of L-lysine in bacteria
metabolism
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meso-diaminopimelate is a biosynthetic precursor of L-lysine in bacteria
metabolism
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diaminopimelate epimerase (DapF) catalyzes the final step in the synthesis of meso-diaminopimelate, an amino acid unique to peptidoglycan, and synthesizes D-glutamate, EC 5.1.1.3
metabolism
the enzyme is involved in L-lysine biosynthesis, where it converts LL-diaminopimelate (LL-DAP) into DL-DAP. In the succinylase pathway, LL-diaminopimelate is synthesized from THDP by succinylation, transamination, and desuccinylation steps, LL-DAP is converted to DL-DAP by the action of DAP epimerase. In contrast, in the mDAP dehydrogenase pathway, DAP dehydrogenase converts THDP into DL-DAP in one step, DAP decarboxylase subsequently catalyzes the decarboxylation of DL-DAP to form L-lysine
metabolism
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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the enzyme is involved in L-lysine biosynthesis, where it converts LL-diaminopimelate (LL-DAP) into DL-DAP. In the succinylase pathway, LL-diaminopimelate is synthesized from THDP by succinylation, transamination, and desuccinylation steps, LL-DAP is converted to DL-DAP by the action of DAP epimerase. In contrast, in the mDAP dehydrogenase pathway, DAP dehydrogenase converts THDP into DL-DAP in one step, DAP decarboxylase subsequently catalyzes the decarboxylation of DL-DAP to form L-lysine
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enzyme belongs to the group of isomerases which are capable of inverting the absolute configuration of a carbon atom in substrates containing one (racemases) or more stereocenters
physiological function
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enzyme is a member of the PLP-independent amino-acid racemases, it catalyzes the penultimate step of lysine biosynthesis in bacteria and plants
physiological function
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(2R,6S)-2,6-diaminopimelic acid, i.e. meso-diaminopimelate, in the pentapeptide of cell wall peptidoglycan provides the attachment site for the inner or outer membrane to peptidoglycan
physiological function
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diaminopimelate epimerase is involved in the biosynthesis of meso-DAP and lysine, which are important precursors for the synthesis of peptidoglycan, housekeeping proteins, and virulence factors in bacteria
physiological function
diaminopimelate isomers are not only intermediates of the lysine biosynthesis diaminopimelate pathway but also essential components of bacterial peptidoglycan
physiological function
redox-mediated modification of cellular proteins confers a respose to changes in the environmental redox potential. CgDapF is regulated by redox-switch modulation, via reversible disulfide bond formation
physiological function
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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redox-mediated modification of cellular proteins confers a respose to changes in the environmental redox potential. CgDapF is regulated by redox-switch modulation, via reversible disulfide bond formation
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physiological function
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diaminopimelate isomers are not only intermediates of the lysine biosynthesis diaminopimelate pathway but also essential components of bacterial peptidoglycan
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dimerization of bacterial diaminopimelate epimerase is essential for catalysis, the enzyme exists in an open, active conformation. The active site of the enzyme resides in a cleft between the two domains with each domain contributing one of the cysteine residues important for catalysis
additional information
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the structure of Chlamydia DAP epimerase exhibits significant remodeling in the substrate-binding pocket, overview
additional information
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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C83 and C221 are catalytic residues
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