| EC |
5.1.1.20 |
| Accepted name: |
L-Ala-D/L-Glu epimerase |
| Reaction: |
L-alanyl-D-glutamate = L-alanyl-L-glutamate |
| Other name(s): |
YkfB; YcjG; AEE; AE epimerase |
| Systematic name: |
L-alanyl-D-glutamate epimerase |
| Comments: |
The enzyme, characterized from the bacteria Escherichia coli and Bacillus subtilis, is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. In vitro the enzyme from Escherichia coli epimerizes several L-Ala-L-X dipeptides with broader specificity than the enzyme from Bacillus subtilis. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Schmidt, D.M., Hubbard, B.K. and Gerlt, J.A. Evolution of enzymatic activities in the enolase superfamily: functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases. Biochemistry 40 (2001) 15707–15715. [DOI] [PMID: 11747447] |
| 2. |
Gulick, A.M., Schmidt, D.M., Gerlt, J.A. and Rayment, I. Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis. Biochemistry 40 (2001) 15716–15724. [DOI] [PMID: 11747448] |
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| [EC 5.1.1.20 created 2015] |
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