Information on EC 5.1.1.13 - aspartate racemase

Word Map on EC 5.1.1.13
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
5.1.1.13
-
RECOMMENDED NAME
GeneOntology No.
aspartate racemase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-aspartate = D-aspartate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
racemization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
-
alanine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
aspartate racemase
Also acts, at half the rate, on L-alanine.
CAS REGISTRY NUMBER
COMMENTARY hide
37237-56-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
NBRC 14252
-
-
Manually annotated by BRENDA team
strain SY
-
-
Manually annotated by BRENDA team
strain SY
-
-
Manually annotated by BRENDA team
strain ATCC 9790, strain IAM 10065, no activity in strain IAM 10067
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Bifidobacterium bifidum
-
-
-
Manually annotated by BRENDA team
no activity in Leuconostoc mesenteroides
-
-
-
Manually annotated by BRENDA team
no activity in Pediococcus pentosaceus
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
-
aspartate racemase regulates adult neurogenesis
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-aspartate
L-aspartate
show the reaction diagram
L-Ala
D-Ala
show the reaction diagram
L-Asp
D-Asp
show the reaction diagram
L-aspartate
D-aspartate
show the reaction diagram
L-Cysteate
D-Cysteate
show the reaction diagram
L-Cysteine sulfinate
D-Cysteine sulfinate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-Asp
D-Asp
show the reaction diagram
-
the enzyme regulates synthesis of the endogenous D-Asp
-
-
?
L-aspartate
D-aspartate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme contains no significant amount of metal
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Nitro-5-thiocyanobenzoate
-
-
5,5'-dithiobis(2-nitrobenzoate)
alpha-methyl-DL-aspartic acid
-
10 mM, 12% inhibition
Amino-oxyacetate
-
complete inhibition
amino-oxyacetic acid
-
-
Citric acid
competitive
D-cycloserine
-
-
D-penicillamine
-
-
GTP
-
non-competitive inhibition
HgCl2
-
0.1 M, complete inhibition, pH 7.0, 30C, 30 min
hydroxylamine
iodoacetamide
-
-
L-Cycloserine
-
-
L-Penicillamine
-
-
N-ethylmaleimide
p-chloromercuribenzoate
-
-
PCMB
-
0.1 M, complete inhibition, pH 7.0, 30C, 30 min
phenylhydrazine
-
-
sodium borhydride
-
-
thiol reagents
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
10 mM ADP increases the activity to 320% of the control
pyridoxal phosphate
-
racemase contains bound pyridoxal phosphate
SH-protecting reagents
-
e.g., 2-mercaptoethanol and dithiothreitol increase activity 2fold
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.94 - 8.7
D-Asp
17.2 - 164
D-Aspartate
13.4 - 35
L-Asp
0.7 - 159
L-aspartate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.4 - 42.9
D-Aspartate
2.6 - 14.9
L-aspartate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.48 - 1.98
ATP
7.4
Citric acid
pH 8.0, 70C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.39
-
for L-aspartate
22.6
-
for D-aspartate
460
-
Vmax of recombinant enzyme, activity is assayed in 500 nl of pyrydoxal 5'-phosphate (100 nM), 0.49 ml of recombinant enzyme (0.5 mg/ml), and 0.01 mL of 1 mM L-aspartate at 37C for 1 h in 10 mM Tris (pH 7.5)
1160
-
70C, pH not specified in the publication
additional information
-
the pituitary gland is the tissue which contains the highest enzymatic activity, with 20.0 EU/mg protein, followed by: testis; brain, liver, kidney and serum, 1 enzyme unit (EU) is defined as the amount of the enzyme capable of generating 1 nmol of D-Asp in 60 min of incubation at 37C and in the assay conditions (0.1 M Tris-HCl,10 mM EDTA, 0.1 M sodium L-aspartate)
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
-
pH 6.5: 59% of maximal activity, pH 8.5: 74% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
-
activity increases with temperature from 37C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
enzyme is purified from foot muscle of Scapharca broughtonii
Manually annotated by BRENDA team
-
no significant seasonal differences in racemase concentration
Manually annotated by BRENDA team
-
concentration of the enzyme in optic lobe is 6fold higher than in the retina
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
gel filtration
27945
-
x * 27945, calculation from nucleotide sequence
30000
-
1 * 30000, SDS-PAGE
37100
-
predicted from cDNA
39000
-
39000, SDS-PAGE
51000 - 63000
-
gel filtration
60000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalytically inactive mutant C82A in complex with citric acid, 2.0 A resolution. Citric acid binds to the catalytic site, which induces a conformational change to close the active site. Residue R48 is responsible for recognizing carboxyl groups of the substrates L-/D-aspartates and stabilizing a reaction intermediate, and L164 is responsible for stabilizing a closed state structure
sitting drop vapour diffusion method at 293 K, space group P21 with a: 65.5 A, b: 58.7 A, c: 67 A and beta 109.6
-
sitting drop vapour diffusion method at 293 K, space groups: P21 with a: 65.5 A, b: 58.7 A, c: 67.0 A, and beta: 109.6, P212121 with a: 68.1 A, b: 135 A and c: 151.5 A, and P3121 with a and b: 80.6 A and c: 70.3 A
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
-
stable
2077
6 - 7
-
30C, 30 min, stable
661647
6 - 9
-
thermal stability shows a bimodal dependence on pH, with minimum stability at pH 7.5, and remarkably stability at pH 6 and pH 8-9. 10 min, pH 8, 66% loss of activity
2075
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
30 min, stable up to 30C in 0.1 M Tes buffer, pH 6.5 containing 4 mM dithiothreitol and 1 mM EDTA
50
-
1 h, about 60% loss of activity, pH 7.2
60
-
30 min, stable up to 60C in presence of 40 mM D-Asp
100
-
thermal stability shows a bimodal dependence on pH, with minimum stability at pH 7.5, and remarkably stability at pH 6 and pH 8-9. 10 min, pH 8, 66% loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
aspartate racemase is purified from the Scapharca broughtonii foot muscle by a procedure that includes sodium sulfate fractionation and blue sepharose column chromatography. The purified enzyme (225 mg) is digested at 25C for 12 h with 80 mg of lysyl endopeptidase in a reaction mixture comprising 50 mM Tris-HCl, pH 8.0, containing 2 M guanidine hydrochloride, and the resulting peptides is resolved by reverse phase high performance liquid chromatography on a capcell Pac C-8 column (0.2 mm x 15 cm) using an acetonitrile gradient in 0.06% trifluoroacetic acid
-
His-tagged aspartate racemase is purified on Talon metal affinity resin
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli
-
enzyme is cloned into pET vector, which is transformed into BL21 Escherichia coli
-
expression in Escherichia coli
expression in Synechocystes PCC 6803 with a His6-tag
-
overexpression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K136W
-
the importance of lysine-136, the presumed proton donor, is highlighted by its mutation to tryptophan, which virtually abolishes racemase activity
additional information
-
the cDNA included an open reading frame of 1017 bp encoding a protein of 338 amino acids, and the deduced amino acid sequence contains a pyridoxal 5'-phosphate-binding motif
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
estimation of age from dentin by using the racemization reaction of Asp
Show AA Sequence (1332 entries)
Please use the Sequence Search for a specific query.