5.1.1.7: diaminopimelate epimerase

This is an abbreviated version!
For detailed information about diaminopimelate epimerase, go to the full flat file.

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 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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Results	in table
8	Activating Compound
37558	AA Sequence
13	Application
1	CAS Registry Number
12	Cloned(Commentary)
2	Cofactor
12	Crystallization (Commentary)
21	General Information
2	General Stability
1	IC50 Value
34	Inhibitors
12	KM Value [mM]
8	Molecular Weight [Da]
16	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
251	Organism
10	Pathway
38	PDB ID
5	pH Optimum
2	pH Range
4	pH Stability
32	Protein Variants
14	Purification (Commentary)
4	Reaction
5	Reaction Type
59	Reference
1	Source Tissue
7	Specific Activity [micromol/min/mg]
1	Storage Stability
60	Substrates and Products (Substrate)
7	Subunits
45	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Range [°C]
8	Turnover Number [1/s]

Reaction

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Reaction on EC 5.1.1.7 - diaminopimelate epimerase

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate

4 entries

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate

two-base mechanism for proton translocation. One, but not both, of the proton acceptor sites is a thiol

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LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate

molecular dynamics simulations show that the configuration of the distal carbon C–6 of L,L-DAP is critical for complex formation since both amino and carboxylate groups are involved in H–bonding interactions with the active site residues. Furthermore, the interactions occurring between the functional groups bonded to the C–2 and some residues of the binding cavity immobilize the ligand in a position appropriate for the epimerization reaction, i.e., exactly in the middle of the two catalytic residues Cys73 and Cys217 as confirmed by DFT (density-functional theory) quantum mechanical computation of the Michaelis complex

Haemophilus influenzae

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675487

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate

molecular mechanism of the enzyme, reversible disulfide bond formation at the active site of CgDapF and disulfide bond-mediated conformational change in CgDapF, domain movement in CgDapF, CgDapF is regulated by redox-switch modulation, via reversible disulfide bond formation, overview

Corynebacterium glutamicum

Q8NP73

749346

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate

molecular mechanism of the enzyme, reversible disulfide bond formation at the active site of CgDapF and disulfide bond-mediated conformational change in CgDapF, domain movement in CgDapF, CgDapF is regulated by redox-switch modulation, via reversible disulfide bond formation, overview

Corynebacterium glutamicum ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025

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