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Literature summary extracted from

  • Schmidt, D.M.; Hubbard, B.K.; 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 (2001), Biochemistry, 40, 15707-15715.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.14.13
-
 Bacillus subtilis
5.1.1.20
-
 Bacillus subtilis
5.1.1.20
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.14.13 0.12
-
 L-Ala-gamma-D-Glu-L-Lys-D-Ala pH and temperature not specified in the publication Bacillus subtilis
3.4.14.13 0.29
-
 L-Ala-gamma-D-Glu-L-Lys pH and temperature not specified in the publication Bacillus subtilis
3.4.14.13 0.31
-
 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala pH and temperature not specified in the publication Bacillus subtilis
5.1.1.20 0.028
-
 L-Ala-D-Asp pH 8.5, 37°C Bacillus subtilis
5.1.1.20 0.13
-
 L-Ala-D-Glu pH 8.5, 37°C Escherichia coli
5.1.1.20 0.19
-
 L-Ala-D-Asp pH 8.5, 37°C Escherichia coli
5.1.1.20 0.32
-
 L-Ala-D-Glu pH 8.5, 37°C Bacillus subtilis
5.1.1.20 0.51
-
 L-Ala-D-Met pH 8.5, 37°C Bacillus subtilis
5.1.1.20 0.69
-
 L-Ala-D-Met pH 8.5, 37°C Escherichia coli
5.1.1.20 1.8
-
 L-Ala-D-Gln pH 8.5, 37°C Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.20 34955
-
 x * 34955, calculated from sequence Escherichia coli
5.1.1.20 34994
-
 x * 34994, electrospray ionization mass spectrometry Escherichia coli
5.1.1.20 39472
-
 x * 39472, calculated from sequence Bacillus subtilis
5.1.1.20 39500
-
 x * 39500, electrospray ionization mass spectrometry Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O Bacillus subtilis the enzyme from is involved in the recycling of the murein peptide L-Ala-D-Glu + L-Lys-D-Ala-D-Ala
-
 ?
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O Bacillus subtilis 168 the enzyme from is involved in the recycling of the murein peptide L-Ala-D-Glu + L-Lys-D-Ala-D-Ala
-
 ?
5.1.1.20 L-Ala-D-Glu Bacillus subtilis the enzyme is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. The murein hydrolases degrade peptidoglycan to the final dipeptide L-Ala-D-Glu. If L-Ala-D-Glu is epimerized to L-Ala-L-Glu, hydrolysis can occur with bacterial dipeptidases L-Ala-L-Glu
-
 r

Organism

EC Number Organism UniProt Comment Textmining
3.4.14.13 Bacillus subtilis O35010
-
-
3.4.14.13 Bacillus subtilis 168 O35010
-
-
5.1.1.20 Bacillus subtilis O34508
-
-
5.1.1.20 Escherichia coli P51981
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.14.13 His-tagged enzyme Bacillus subtilis
5.1.1.20
-
 Bacillus subtilis
5.1.1.20
-
 Escherichia coli

Storage Stability

EC Number Storage Stability Organism
3.4.14.13 -20°C, 40% glycerol, significant loss of activity Bacillus subtilis
3.4.14.13 4°C, stable in absence of glycerol for 48h Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys + H2O
-
 Bacillus subtilis L-Ala-D-Glu + L-Lys
-
 ?
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys + H2O
-
 Bacillus subtilis 168 L-Ala-D-Glu + L-Lys
-
 ?
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys-D-Ala + H2O
-
 Bacillus subtilis L-Ala-D-Glu + L-Lys-D-Ala
-
 ?
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys-D-Ala + H2O
-
 Bacillus subtilis 168 L-Ala-D-Glu + L-Lys-D-Ala
-
 ?
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O the enzyme from is involved in the recycling of the murein peptide Bacillus subtilis L-Ala-D-Glu + L-Lys-D-Ala-D-Ala
-
 ?
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O the enzyme is specific for the gamma-D-Glu-L-Lys bond. No activity with L-Ala-D-Glu-L-Lys-D-Ala-D-Ala or L-Ala-gamma-L-Glu-L-Lys-D-Ala-D-Ala Bacillus subtilis L-Ala-D-Glu + L-Lys-D-Ala-D-Ala
-
 ?
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O the enzyme from is involved in the recycling of the murein peptide Bacillus subtilis 168 L-Ala-D-Glu + L-Lys-D-Ala-D-Ala
-
 ?
3.4.14.13 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O the enzyme is specific for the gamma-D-Glu-L-Lys bond. No activity with L-Ala-D-Glu-L-Lys-D-Ala-D-Ala or L-Ala-gamma-L-Glu-L-Lys-D-Ala-D-Ala Bacillus subtilis 168 L-Ala-D-Glu + L-Lys-D-Ala-D-Ala
-
 ?
5.1.1.20 Gly-L-Glu
-
 Escherichia coli Gly-D-Glu
-
 r
5.1.1.20 L-Ala-D-Asp
-
 Bacillus subtilis L-Ala-L-Asp
-
 r
5.1.1.20 L-Ala-D-Asp
-
 Escherichia coli L-Ala-L-Asp
-
 r
5.1.1.20 L-Ala-D-Gln
-
 Escherichia coli L-Ala-L-Gln
-
 r
5.1.1.20 L-Ala-D-Glu
-
 Bacillus subtilis L-Ala-L-Glu
-
 r
5.1.1.20 L-Ala-D-Glu
-
 Escherichia coli L-Ala-L-Glu
-
 r
5.1.1.20 L-Ala-D-Glu the enzyme is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. The murein hydrolases degrade peptidoglycan to the final dipeptide L-Ala-D-Glu. If L-Ala-D-Glu is epimerized to L-Ala-L-Glu, hydrolysis can occur with bacterial dipeptidases Bacillus subtilis L-Ala-L-Glu
-
 r
5.1.1.20 L-Ala-D-Met
-
 Bacillus subtilis L-Ala-L-Met
-
 r
5.1.1.20 L-Ala-D-Met
-
 Escherichia coli L-Ala-L-Met
-
 r
5.1.1.20 L-Ala-L-Ala
-
 Escherichia coli L-Ala-D-Ala
-
 r
5.1.1.20 L-Ala-L-Asn
-
 Escherichia coli L-Ala-D-Asn
-
 r
5.1.1.20 L-Ala-L-Asp
-
 Bacillus subtilis L-Ala-D-Asp
-
 r
5.1.1.20 L-Ala-L-Asp
-
 Escherichia coli L-Ala-D-Asp
-
 r
5.1.1.20 L-Ala-L-Gln
-
 Escherichia coli L-Ala-D-Gln
-
 r
5.1.1.20 L-Ala-L-Glu
-
 Bacillus subtilis L-Ala-D-Glu
-
 r
5.1.1.20 L-Ala-L-Glu
-
 Escherichia coli L-Ala-D-Glu
-
 r
5.1.1.20 L-Ala-L-His L-Ala-L-His is epimerized by YcjG at pH 8 but not at pH 6 Escherichia coli L-Ala-D-His
-
 r
5.1.1.20 L-Ala-L-Ile
-
 Escherichia coli L-Ala-D-Ile
-
 r
5.1.1.20 L-Ala-L-Leu
-
 Bacillus subtilis L-Ala-D-Leu
-
 r
5.1.1.20 L-Ala-L-Leu
-
 Escherichia coli L-Ala-D-Leu
-
 r
5.1.1.20 L-Ala-L-Met
-
 Bacillus subtilis L-Ala-D-Met
-
 r
5.1.1.20 L-Ala-L-Met
-
 Escherichia coli L-Ala-D-Met
-
 r
5.1.1.20 L-Ala-L-Phe
-
 Escherichia coli L-Ala-D-Phe
-
 r
5.1.1.20 L-Ala-L-Ser
-
 Bacillus subtilis L-Ala-D-Ser
-
 r
5.1.1.20 L-Ala-L-Ser
-
 Escherichia coli L-Ala-D-Ser
-
 r
5.1.1.20 L-Ala-L-Thr
-
 Escherichia coli L-Ala-D-Thr
-
 r
5.1.1.20 L-Ala-L-Trp
-
 Escherichia coli L-Ala-D-Trp
-
 r
5.1.1.20 L-Ala-L-Tyr
-
 Escherichia coli L-Ala-D-Tyr
-
 r
5.1.1.20 L-Ala-L-Val
-
 Escherichia coli L-Ala-D-Val
-
 r
5.1.1.20 L-Phe-L-Glu
-
 Escherichia coli L-Phe-D-Glu
-
 r
5.1.1.20 L-Pro-L-Glu
-
 Bacillus subtilis L-Pro-D-Glu
-
 r
5.1.1.20 L-Ser-L-Glu
-
 Bacillus subtilis L-Ser-D-Glu
-
 r
5.1.1.20 L-Ser-L-Glu
-
 Escherichia coli L-Ser-D-Glu
-
 r
5.1.1.20 additional information no activity with L-Ala-L-Arg, L-Ala-L-Lys, L-Ala-L-Pro, L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala Bacillus subtilis ?
-
 ?
5.1.1.20 additional information no activity with L-Ala-L-Arg, L-Ala-L-Lys, L-Ala-L-Pro, L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.1.1.20 ? x * 34955, calculated from sequence Escherichia coli
5.1.1.20 ? x * 34994, electrospray ionization mass spectrometry Escherichia coli
5.1.1.20 ? x * 39472, calculated from sequence Bacillus subtilis
5.1.1.20 ? x * 39500, electrospray ionization mass spectrometry Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
3.4.14.13 gamma-D-glutamyl-L-lysine endopeptidase
-
 Bacillus subtilis
3.4.14.13 YkfC
-
 Bacillus subtilis
5.1.1.20 AEE
-
 Bacillus subtilis
5.1.1.20 YcjG
-
 Escherichia coli
5.1.1.20 YkfB
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.14.13 37
-
 assay at Bacillus subtilis
5.1.1.20 37
-
 assay at Bacillus subtilis
5.1.1.20 37
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.14.13 1.2
-
 L-Ala-gamma-D-Glu-L-Lys pH and temperature not specified in the publication Bacillus subtilis
3.4.14.13 2.6
-
 L-Ala-gamma-D-Glu-L-Lys-D-Ala pH and temperature not specified in the publication Bacillus subtilis
3.4.14.13 5.7
-
 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala pH and temperature not specified in the publication Bacillus subtilis
5.1.1.20 0.053
-
 L-Ala-D-Asp pH 8.5, 37°C Bacillus subtilis
5.1.1.20 1.1
-
 L-Ala-D-Met pH 8.5, 37°C Bacillus subtilis
5.1.1.20 1.9
-
 L-Ala-D-Met pH 8.5, 37°C Escherichia coli
5.1.1.20 3.3
-
 L-Ala-D-Gln pH 8.5, 37°C Escherichia coli
5.1.1.20 10
-
 L-Ala-D-Glu pH 8.5, 37°C Escherichia coli
5.1.1.20 15
-
 L-Ala-D-Glu pH 8.5, 37°C Bacillus subtilis
5.1.1.20 17
-
 L-Ala-D-Asp pH 8.5, 37°C Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.14.13 8.5
-
 assay at Bacillus subtilis
5.1.1.20 8.5
-
 assay at Bacillus subtilis
5.1.1.20 8.5
-
 assay at Escherichia coli

General Information

EC Number General Information Comment Organism
3.4.14.13 physiological function the enzyme is involved in the recycling of the murein peptide Bacillus subtilis
5.1.1.20 physiological function the enzyme is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component Bacillus subtilis
5.1.1.20 physiological function the enzyme is involved in the recycling of the murein peptide, of which L-Ala-D-Glu is a component Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.4.14.13 4.1
-
 L-Ala-gamma-D-Glu-L-Lys pH and temperature not specified in the publication Bacillus subtilis
3.4.14.13 18
-
 L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala pH and temperature not specified in the publication Bacillus subtilis
3.4.14.13 22
-
 L-Ala-gamma-D-Glu-L-Lys-D-Ala pH and temperature not specified in the publication Bacillus subtilis
5.1.1.20 1.8
-
 L-Ala-D-Gln pH 8.5, 37°C Escherichia coli
5.1.1.20 1.9
-
 L-Ala-D-Asp pH 8.5, 37°C Bacillus subtilis
5.1.1.20 2.2
-
 L-Ala-D-Met pH 8.5, 37°C Bacillus subtilis
5.1.1.20 2.8
-
 L-Ala-D-Met pH 8.5, 37°C Escherichia coli
5.1.1.20 47
-
 L-Ala-D-Glu pH 8.5, 37°C Bacillus subtilis
5.1.1.20 77
-
 L-Ala-D-Glu pH 8.5, 37°C Escherichia coli
5.1.1.20 89
-
 L-Ala-D-Asp pH 8.5, 37°C Escherichia coli