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
-
ll-dap
-
plp-independent
- meso-diaminopimelate
-
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 (Substrates Products
Substrates Products on EC 5.1.1.7 - diaminopimelate epimerase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,6S)-2,6-diaminoheptanedioate
meso-diaminoheptanedioate
-
-
-
?
DL-3-fluoro-2,6-diaminopimelic acid
tetrahydrodipicolinic acid + HF
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rapid elimination, enamine product is formed which spontaneously cyclizes to tetrahydrodipicolinic acid
-
?
LL-3-fluoro-2,6-diaminopimelic acid
tetrahydrodipicolinic acid + HF
-
slow elimination of HF
-
?
LL-oxa-diaminopimelic acid
meso-oxa-diaminopimelic acid
-
-
-
?
LL-2,6-Diaminoheptanedioate
?
-
enzyme active in two of three possible pathways for synthesis of L-Lys, acetyltransferase pathway and succinyltransferase pathway. Not active in D-diaminopimelate dehydrogenase variant
-
-
?
LL-2,6-Diaminoheptanedioate
?
-
enzyme of the diaminopimelic acid pathway for biosynthesis of Lys
-
-
?
LL-2,6-Diaminoheptanedioate
meso-Diaminoheptanedioate
-
-
-
r
LL-2,6-Diaminoheptanedioate
meso-Diaminoheptanedioate
Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025
-
-
-
r
LL-2,6-Diaminoheptanedioate
meso-Diaminoheptanedioate
-
-
-
?
LL-2,6-Diaminoheptanedioate
meso-Diaminoheptanedioate
-
-
-
r
LL-2,6-Diaminoheptanedioate
meso-Diaminoheptanedioate
-
-
-
-
?
LL-2,6-Diaminoheptanedioate
meso-Diaminoheptanedioate
-
r, between 25°C and 45°C at pH 7.0, the equilibrium mixture contains 65% meso-isomer and 35% LL-isomer
-
?
LL-2,6-Diaminoheptanedioate
meso-Diaminoheptanedioate
-
-
-
?
LL-2,6-diaminoheptanedioate
meso-diaminopimelate
stereo-conversion, the product complex (Enzyme/meso-diaminopimelate) is less stable than the reactant complex (Enzyme/LL-diaminopimelate)
-
-
r
LL-2,6-diaminoheptanedioate
meso-diaminopimelate
stereo-inversion
the meso-isomer of diaminopimelic acid, a precursor of L-lysine, is a key component of the pentapeptide linker in bacterial peptidoglycan
-
?
LL-2,6-diaminoheptanedioate
meso-diaminopimelate
stereo-inversion
the meso-isomer of diaminopimelic acid, a precursor of L-lysine, is a key component of the pentapeptide linker in bacterial peptidoglycan
-
?
meso-diaminoheptanedioate
LL-2,6-diaminoheptanedioate
-
-
-
r
meso-diaminoheptanedioate
LL-2,6-diaminoheptanedioate
-
-
-
r
additional information
?
-
ligand binding to a cleft between the two domains of the enzyme is accompanied by domain closure with strictly conserved cysteine residues, Cys99 and Cys254, positioned to perform acid/base catalysis via a carbanion stabilization mechanism on the stereogenic alpha-carbon atom of the amino acid. Stereochemical control in catalysis is achieved by means of a highly symmetric catalytic site that can accommodate both the L and D stereogenic centers of DAP at the proximal site, whereas specific interactions at the distal site require only the L configuration
-
-
?
additional information
?
-
-
ligand binding to a cleft between the two domains of the enzyme is accompanied by domain closure with strictly conserved cysteine residues, Cys99 and Cys254, positioned to perform acid/base catalysis via a carbanion stabilization mechanism on the stereogenic alpha-carbon atom of the amino acid. Stereochemical control in catalysis is achieved by means of a highly symmetric catalytic site that can accommodate both the L and D stereogenic centers of DAP at the proximal site, whereas specific interactions at the distal site require only the L configuration
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-
?
additional information
?
-
-
Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase, EC 5.1.1.3, and diaminopimelate epimerase activities. DAP and glutamate appear to be competitive substrates, indicating that they share an active site despite the racemase reaction requiring the pyridoxal 5'-phosphate cofactor
-
-
?
additional information
?
-
no activity with DD-2,6-diaminoheptanedioate. Development of a simple method using thin-layer chromatography, in methanol/water (64:36) and with ninhydrin detection, and chiral column chromatography to allow preparation of pure diaminopimelate isomers and detect products, respectively, overview
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-
?
additional information
?
-
no activity with DD-2,6-diaminoheptanedioate. Development of a simple method using thin-layer chromatography, in methanol/water (64:36) and with ninhydrin detection, and chiral column chromatography to allow preparation of pure diaminopimelate isomers and detect products, respectively, overview
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-
?
