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Information on EC 3.4.14.13 - gamma-D-glutamyl-L-lysine dipeptidyl-peptidase and Organism(s) Bacillus subtilis and UniProt Accession O35010

for references in articles please use BRENDA:EC3.4.14.13
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Bacillus subtilis
UNIPROT: O35010 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
The enzyme releases L-Ala-gamma-D-Glu dipeptides from cell wall peptides via cleavage of an L-Ala-gamma-D-Glu-/-L-Lys bond
Synonyms
BcYkfC, gamma-D-glutamyl-L-lysine endopeptidase, YkfC, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
gamma-D-glutamyl-L-lysine endopeptidase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Ala-gamma-D-Glu-L-Lys + H2O
L-Ala-D-Glu + L-Lys
show the reaction diagram
-
-
-
?
L-Ala-gamma-D-Glu-L-Lys-D-Ala + H2O
L-Ala-D-Glu + L-Lys-D-Ala
show the reaction diagram
-
-
-
?
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O
L-Ala-D-Glu + L-Lys-D-Ala-D-Ala
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala + H2O
L-Ala-D-Glu + L-Lys-D-Ala-D-Ala
show the reaction diagram
the enzyme from is involved in the recycling of the murein peptide
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29
L-Ala-gamma-D-Glu-L-Lys
pH and temperature not specified in the publication
0.12
L-Ala-gamma-D-Glu-L-Lys-D-Ala
pH and temperature not specified in the publication
0.31
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
L-Ala-gamma-D-Glu-L-Lys
pH and temperature not specified in the publication
2.6
L-Ala-gamma-D-Glu-L-Lys-D-Ala
pH and temperature not specified in the publication
5.7
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala
pH and temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1
L-Ala-gamma-D-Glu-L-Lys
pH and temperature not specified in the publication
22
L-Ala-gamma-D-Glu-L-Lys-D-Ala
pH and temperature not specified in the publication
18
L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in the recycling of the murein peptide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 40% glycerol, significant loss of activity
4°C, stable in absence of glycerol for 48h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged enzyme
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Biochemistry
40
15707-15715
2001
Bacillus subtilis (O35010), Bacillus subtilis 168 (O35010)
Manually annotated by BRENDA team