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Information on EC 5.1.1.7 - diaminopimelate epimerase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LFG2

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.1 Acting on amino acids and derivatives
                5.1.1.7 diaminopimelate epimerase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9LFG2 not found.
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
diaminopimelate epimerase, dap epimerase, diaminopimelic acid epimerase, mtdapf, cgdapf, dapfct, dap-epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DAP epimerase
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-
-
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DAP-epimerase
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-
-
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Diaminopimelic acid epimerase
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-
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Diaminopimelic epimerase
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-
-
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Epimerase, diaminopimelate
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-
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LL-Diaminopimelate epimerase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
LL-2,6-diaminoheptanedioate 2-epimerase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-22-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(4-amino-4-carboxybutyl)-aziridine-2-carboxylate
substrate mimic, irreversible inhibition
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DAPF_ARATH
362
0
38984
Swiss-Prot
Chloroplast (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with two different isomers of inhibitor 2-(4-amino-4-carboxybutyl)-aziridine-2-carboxylate, at 1.95 and 2.3 A resolution. 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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pillai, B.; Moorthie, V.A.; van Belkum, M.J.; Marcus, S.L.; Cherney, M.M.; Diaper, C.M.; Vederas, J.C.; James, M.N.
Crystal structure of diaminopimelate epimerase from Arabidopsis thaliana, an amino acid racemase critical for l-lysine biosynthesis
J. Mol. Biol.
385
580-594
2009
Arabidopsis thaliana (Q9LFG2), Arabidopsis thaliana
Manually annotated by BRENDA team