Enzyme

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EC Tree
     5. Isomerases
        5.1 Racemases and epimerases
            5.1.1 Acting on amino acids and derivatives
ID:5.1.1.5
Description:Lysine racemase.
Cath: 3.20.20.10; 2.40.37.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.1.1.5
BRENDA Enzyme Link: BRENDA 5.1.1.5
KEGG Enzyme Link: KEGG5.1.1.5
BioCyc Enzyme Link: BioCyc 5.1.1.5
ExPASy Enzyme Link: ExPASy5.1.1.5
EC2PDB Enzyme Link: EC2PDB 5.1.1.5
ExplorEnz Enzyme Link: ExplorEnz 5.1.1.5
PRIAM enzyme-specific profiles Link: PRIAM 5.1.1.5
IntEnz Enzyme Link: IntEnz 5.1.1.5
MEDLINE Enzyme Link: MEDLINE 5.1.1.5
MSA:

5.1.1.5;

Phylogenetic Tree:

5.1.1.5;

Uniprot:
M-CSA:
RHEA:22864 L-lysine = D-lysine
RULE(radius=1)
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural basis for the broad specificity of a new family of amino-acid racemases.Espaillat A, Carrasco-López C, Bernardo-García N, Pietrosemoli N, Otero LH, Álvarez L, de Pedro MA, Pazos F, Davis BM, Waldor MK, Hermoso JA, Cava F2014 Jan24419381
A periplasmic, pyridoxal-5'-phosphate-dependent amino acid racemase in Pseudomonas taetrolens.Matsui D, Oikawa T, Arakawa N, Osumi S, Lausberg F, Stäbler N, Freudl R, Eggeling L2009 Jul19300994