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
-
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
5.1.1.7 diaminopimelate epimeraseAdvanced search results
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results (Engineering
Engineering on EC 5.1.1.7 - diaminopimelate epimerase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
N159A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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site-directed mutagenesis, nearly inactive mutant
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N74A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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site-directed mutagenesis, nearly inactive mutant
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N85A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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site-directed mutagenesis, nearly inactive mutant
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R213A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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site-directed mutagenesis, nearly inactive mutant
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T223A
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
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site-directed mutagenesis, nearly inactive mutant
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Y268A
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site-directed mutagenesis, the monomeric mutant is catalytically inactive
C217A
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mutant enzyme is inactive as epimerase, catalyzes elimination of HF via abstraction of the C-2 hydrogen from L,L-3-fluoro-2,6-diaminopimelate, incapable of catalyzing HF elimination from D,L-3-fluoro-2,6-diaminopimelate
C217S
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catalyzes epimerization of L,L-diaminopimelate at 2% of the activity of the wild-type enzyme,catalyzes HF elimination from L,L-3-fluoro-2,6-diaminopimelate and D,L-3-fluoro-2,6-diaminopimelate
C73A
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mutant enzyme is inactive as epimerase, catalyzes elimination of HF via abstraction of the C-2 hydrogen. Mutant enzyme is able to rapidly catalyze elimination of the D,L-3-fluoro-2,6-diaminopimelate and is unable to catalyze elimination with the L,L-3-fluoro-2,6-diaminopimelate
C73S
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epimerization of L,L-diaminopimelate at 3% of the activity of the wild-type enzyme, catalyzes HF elimination from L,L-3-fluoro-2,6-diaminopimelate and D,L-3-fluoro-2,6-diaminopimelate
C73S/C217S
C87S
severely compromised catalytic efficiency despite decrease in Km value
C87S
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severely compromised catalytic efficiency despite decrease in Km value
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additional information
C73S/C217S
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mutant enzyme is inactive as epimerase, slow elimination of HF from D,L-3-fluoro-2,6-diaminopimelate and L,L-3-fluoro-2,6-diaminopimelate
C73S/C217S
in order to prevent C73 and C217 of DAP epimerase from oxidation to a disulfide prior to crystallization, DAP epimerase mutants C73S and C217S from Haemophilus influenzae are generated by site-directed mutagenesis
additional information
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a recombinant DapF is generated consisting of silent mutation of the first 10 codons of the open reading frame. single nucleotide substitutions are incorporated without changing product composition in the first 30 nucleotides of the dapF open reading frame,in order to disrupt any secondary structure-promoting sequences present. this significantly increases the yield of the enzyme
additional information
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a recombinant DapF is generated consisting of silent mutation of the first 10 codons of the open reading frame. single nucleotide substitutions are incorporated without changing product composition in the first 30 nucleotides of the dapF open reading frame,in order to disrupt any secondary structure-promoting sequences present. this significantly increases the yield of the enzyme
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