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Information on EC 4.3.1.15 - Diaminopropionate ammonia-lyase
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4.3.1.15 Diaminopropionate ammonia-lyaseIUBMB Comments
A pyridoxal phosphate enzyme. Active towards both D- and L-diaminopropanoate. D- and L-serine are poor substrates.
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Word Map
- 4.3.1.15
- typhimurium
- 5'-phosphate
-
plp-dependent
- l-2,3-diaminopropionate
-
alpha,beta-elimination
-
d-isomer
-
neurotoxins
-
monoclinic
-
l-forms
- dehydratase
-
tetragonal
-
pseudomonad
-
etch
- d-serine
-
monovalent
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
2,3-Diaminopropionate:ammonia-lyase, alpha,beta-Diaminopropionate ammonia-lyase, ammonia-lyase, diaminopropionate, DAP ammonia-lyase, DAPAL, Diaminopropionatase, diaminopropionate ammonia lyase, diaminopropionate ammonia-lyase, DpaL, EcDAPAL, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-Diaminopropionate:ammonia-lyase
-
-
-
-
alpha,beta-Diaminopropionate ammonia-lyase
-
-
-
-
ammonia-lyase, diaminopropionate
-
-
-
-
DAP ammonia-lyase
-
-
-
-
DAPAL
Diaminopropionatase
-
-
-
-
diaminopropionate ammonia lyase
diaminopropionate ammonia-lyase
DpaL
L-Diaminopropionate ammonia-lyase
-
-
-
-
diaminopropionate ammonia lyase
-
diaminopropionate ammonia lyase
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3-diaminopropanoate + H2O = pyruvate + 2 NH3
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination of NH3
elimination of NH3
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
2,3-diaminopropanoate ammonia-lyase (adding water; pyruvate-forming)
A pyridoxal phosphate enzyme. Active towards both D- and L-diaminopropanoate. D- and L-serine are poor substrates.
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CAS REGISTRY NUMBER
COMMENTARY
51901-19-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
-
-
-
?
DL-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
-
-
-
?
L-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
-
-
-
?
additional information
?
-
-
the enzyme is induced only by L-2,3-diaminopropionate or D-2,3-diaminopropanoate
-
-
-
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
specific role for the enzyme in degrading 2,3-diaminopropanoate to avoid metabolic stress
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
diaminopropionate ammonia-lyase-dependent degradation of 2,3-diaminopropanoate to pyruvate proceeds through an unbound 2-aminoacrylate intermediate
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
Salmonella enterica DM14828
specific role for the enzyme in degrading 2,3-diaminopropanoate to avoid metabolic stress
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
Salmonella enterica DM14828
diaminopropionate ammonia-lyase-dependent degradation of 2,3-diaminopropanoate to pyruvate proceeds through an unbound 2-aminoacrylate intermediate
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + NH3
-
precursor of a neurotoxin in Lathyrus sativus seed extracts
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + NH3
-
precursor of a neurotoxin in Lathyrus sativus seed extracts
-
-
?
D-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
-
the enzyme degrades both the D and L forms of diaminopropionic acid. A phosphate group is located in the active site of the enzyme and expulsion of this phosphate is probably essential to bring Asp125 to a conformation suitable for proton abstraction from the substrate
-
-
?
D-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
the enzyme degrades both the D and L forms of diaminopropionic acid. A phosphate group is located in the active site of the enzyme and expulsion of this phosphate is probably essential to bring Asp125 to a conformation suitable for proton abstraction from the substrate
-
-
?
D-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
only 12% of the activity with L-2,3-diaminopropanoate
-
-
D-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
-
D-serine
pyruvate + NH3
-
-
-
?
D-serine + H2O
pyruvate + NH3
-
-
-
?
DL-2,3-diaminopropanoate + H2O
pyruvate + NH3
-
-
-
?
L-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
-
the enzyme degrades both the D and L forms of diaminopropionic acid. A phosphate group is located in the active site of the enzyme and expulsion of this phosphate is probably essential to bring Asp125 to a conformation suitable for proton abstraction from the substrate
-
-
?
L-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
the enzyme degrades both the D and L forms of diaminopropionic acid. A phosphate group is located in the active site of the enzyme and expulsion of this phosphate is probably essential to bring Asp125 to a conformation suitable for proton abstraction from the substrate
-
-
?
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
-
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
L-serine
pyruvate + NH3
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is induced only by L-2,3-diaminopropionate or D-2,3-diaminopropanoate
-
-
-
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
P40817
specific role for the enzyme in degrading 2,3-diaminopropanoate to avoid metabolic stress
-
-
?
2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
Salmonella enterica DM14828
P40817
specific role for the enzyme in degrading 2,3-diaminopropanoate to avoid metabolic stress
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
contains 2 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per mol of enzyme; Km: 0.025 mM
pyridoxal 5'-phosphate
-
dependent on. Pyridoxal 5'-phosphate is covalently attached to Lys78 via a Schiff base linkage in the cleft between large and a small domain of the protomer
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
-
higher activity of the enzyme in the presence of K+ when compared to Na+
KCl
-
addition of increasing concentrations (higher than 10 mM) enhances the activity by 10fold
Na+
-
higher activity of the enzyme in the presence of K+ when compared to Na+
NaCl
-
addition of increasing concentrations enhances the activity by 2fold
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.685
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
pH 8.0, 28°C
0.284
L-cysteine
-
pH 7.4, 30°C, mutant T385D sDAPL
0.74
2,3-Diaminopropionate
-
wild type enzyme, 0.680 using Lathyrus sativus seed extracts as substrate
0.741
2,3-Diaminopropionate
-
recombinant enzyme, 0.683 using Lathyrus sativus seed extracts as substrate
0.05
D-2,3-diaminopropanoate
-
wild-type, pH and temperature not specified in the publication
0.28
D-2,3-diaminopropanoate
-
pH 7.5, 37°C
0.282
D-2,3-diaminopropanoate
-
pH 7.4, 30°C, sDAPL
0.293
D-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D194S sDAPL
0.346
D-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D125S sDAPL
12.9
D-2,3-diaminopropanoate
-
mutant D189N, pH and temperature not specified in the publication
0.375
D-serine
-
pH 7.4, 30°C, mutant T385S sDAPL
0.6
D-serine
-
pH 7.4, 30°C, mutant T385D sDAPL
0.014
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant C271V sDAPL
0.279
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, untagged sDAPL
0.3
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, sDAPL
0.33
DL-2,3-diaminopropanoate
-
pH 7.5, 37°C
0.382
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant T385S sDAPL
0.43
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant C299V sDAPL
0.52
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant T385D sDAPL
0.03
L-2,3-diaminopropanoate
-
wild-type, pH and temperature not specified in the publication
0.24
L-2,3-diaminopropanoate
-
pH 7.5, 37°C
0.246
L-2,3-diaminopropanoate
-
pH 7.4, 30°C, sDAPL
0.3
L-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D125S sDAPL
0.378
L-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D194S sDAPL
0.412
L-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D125E sDAPL
0.57
L-2,3-diaminopropanoate
-
mutant D120N, pH and temperature not specified in the publication
11.5
L-2,3-diaminopropanoate
-
mutant D189N, pH and temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2
L-cysteine
-
pH 7.4, 30°C, mutant T385D sDAPL
0.35
D-2,3-diaminopropanoate
-
mutant D189N, pH and temperature not specified in the publication
7.83
D-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D125S sDAPL
26
D-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D194S sDAPL
42.5
D-2,3-diaminopropanoate
-
pH 7.5, 37°C
44.58
D-2,3-diaminopropanoate
-
wild-type, pH and temperature not specified in the publication
375.8
D-2,3-diaminopropanoate
-
pH 7.4, 30°C, sDAPL
10.5
D-serine
-
pH 7.4, 30°C, mutant T385S sDAPL
34.17
D-serine
-
pH 7.4, 30°C, mutant T385D sDAPL
34
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant C271V sDAPL
42
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant T385D sDAPL
51.67
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant T385S sDAPL
57
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant C299V sDAPL
60.17
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, sDAPL
69.17
DL-2,3-diaminopropanoate
-
pH 7.4, 30°C, untagged sDAPL
0.18
L-2,3-diaminopropanoate
-
mutant D189N, pH and temperature not specified in the publication
2.67
L-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D194S sDAPL
3.05
L-2,3-diaminopropanoate
-
mutant D120N, pH and temperature not specified in the publication
20.83
L-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D125E sDAPL
24.6
L-2,3-diaminopropanoate
-
wild-type, pH and temperature not specified in the publication
37.33
L-2,3-diaminopropanoate
-
pH 7.4, 30°C, mutant D125S sDAPL
42.83
L-2,3-diaminopropanoate
-
pH 7.4, 30°C, sDAPL
43.3
L-2,3-diaminopropanoate
-
pH 7.5, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0266
D-2,3-diaminopropanoate
-
mutant D189N, pH and temperature not specified in the publication
151.7
D-2,3-diaminopropanoate
-
pH 7.5, 37°C
890
D-2,3-diaminopropanoate
-
wild-type, pH and temperature not specified in the publication
0.001
L-2,3-diaminopropanoate
-
mutant D189N, pH and temperature not specified in the publication
5.35
L-2,3-diaminopropanoate
-
mutant D120N, pH and temperature not specified in the publication
180.4
L-2,3-diaminopropanoate
-
pH 7.5, 37°C
820
L-2,3-diaminopropanoate
-
wild-type, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.346
-
of the recombinant enzyme in crude extracts
0.351
-
of the wild type enzyme in crude extracts
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
drastic reduction in activity above pH 11, below pH 6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Salmonella enterica DM14828
the strain is generated from Salmonella enterica serovar typhimurium LT2
SwissProt
brenda
the strain is generated from Salmonella enterica serovar typhimurium LT2
SwissProt
brenda
PU011, produces enzyme when grown on minimal medium containing 2,3-diaminoproprionic acid
-
-
brenda
recombinant enzyme, expression in Escherichia coli
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
malfunction
-
deletion shows loss of growth on DL-DAP, confirming that ygeX is the locus encoding DAPAL. Inhibition by DL-DAP is rescued by transforming the strains with plasmids containing the ygeX gene encoding DAPAL or supplementing the medium with casamino acids
malfunction
deletion shows loss of growth on DL-DAP, confirming that STM1002 is the locus encoding DAPAL. Inhibition by DL-DAP is rescued by transforming the strains with plasmids containing the STM1002 gene encoding DAPAL or supplementing the medium with casamino acids
metabolism
specific role for the enzyme in degrading 2,3-diaminopropanoate to avoid metabolic stress
metabolism
Salmonella enterica DM14828
-
specific role for the enzyme in degrading 2,3-diaminopropanoate to avoid metabolic stress
-
Show AA Sequence and Transmembrane Helices (1957 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
43000
44000
89000
-
equilibrium ultracentrifugation
43000
-
SDS-PAGE of wild type and recombinant protein
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
the enzyme is active as a dimer, it has a tendency to form a higher oligomer at high concentrations
dimer
-
the enzyme is active as a dimer, it has a tendency to form a higher oligomer at high concentrations
-
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structure of DAPAL from Escherichia coli (EcDAPAL) in tetragonal and monoclinic forms at 2.0 and 2.2 A resolutions is shown
-
microbatch method, the three-dimensional X-ray crystal structure of the enzyme is determined at 2.5 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C265S
-
Tm-value of the mutant enzyme is 60°C, compared to 65°C for the wild-type enzyme. The activity of the C291S mutant is higher than that of C265S mutant
C291S
-
Tm-value of the mutant enzyme is 68°C, compared to 65°C for the wild-type enzyme. The activity of the C291S mutant is higher than that of C265S mutant
D120N
-
mutant shows no reaction with D-DAP, Km (L-DAP) increased compared to wild-type, kcat decreased
D189N
-
Km (D-DAP) and (L-DAP) increased compared to wild-type, kcat decreased
C271V
C299V
D125E
-
mutant does not show any activity with D-DAP at all
D125S
-
kcat value in mutant is reduced by 5.4fold for D-DAP compared to wild-type
D194P
-
mutant does not show any activity with either L-DAP or D-DAP. Kd for D-DAP shows a 5fold increase in mutant compared to wild-type. L-DAP does not bind at all to mutant D194P
D194S
-
mutant exhibits an 16fold decrease in kcat with L-DAP whereas activity with D-DAP is reduced only by factor 1.7 compared to wild-type
T385D
-
kcat value with DL-DAP as substrate is 69% of wild-type. Km value for D-Ser doubled in T385D mutant whereas the kcat value increased by 7fold
T385S
-
kcat value with DL-DAP as substrate is 86% of wild-type. Mutant exhibits a 2fold higher Kcat with D-Ser compared to wild-type
C271V
-
mutation results in a 47fold increase in Km and 1.5fold reduction in Kcat with respect to the wild type enzyme when DL-2,3-diaminopropanoate is used as substrate
-
C299V
-
mutation does not effect the activity
-
C271V
-
Km for DL-DAP is 47fold higher compared to wild-type and kcat decreased by 1.5fold compared to wild-type.In contrast to wild-type C271V sDAPAL exhibits only 2fold stimulation in activity even when a high concentration of KCl is used
C271V
-
mutation results in a 47fold increase in Km and 1.5fold reduction in Kcat with respect to the wild type enzyme when DL-2,3-diaminopropanoate is used as substrate
C299V
-
kcat and Km for DL-DAP are similar to wild-type
C299V
-
mutation does not effect the activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
55
-
pH 7.0, 10 min, 50% loss of activity
60
60
-
pH 7.0, 10 min, 90% loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% v/v glycerol, 10 mM potassium phosphate, pH 7.0, 0.01 mM pyridoxal 5'-phosphate, 0.1 mM dithiothreitol, 0.1 mM Na2EDTA, stable for at least 2 months
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
-
expression in Escherichia coli PU018
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of dpaL and protein production are specifically induced in Salmonella enterica when exposed to 2,3-diaminopropanoate
expression of dpaL and protein production are specifically induced in Salmonella enterica when exposed to 2,3-diaminopropanoate
expression of dpaL and protein production are specifically induced in Salmonella enterica when exposed to 2,3-diaminopropanoate
Salmonella enterica DM14828
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
about 60% reconstitution of apoenzyme by addition of pyridoxal 5'-phosphate
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
a specific enzymatic procedure for the determination of neurotoxic components, derivatives of L-2,3-diaminopropanoate with diaminopropanonate ammonia-lyase
medicine
medicine
-
nonvirulent Salmonella typhimurium PU011 can be used for the production of the enzyme to detoxify the neurotoxin 3-oxalyl and 2,3-dioxalyl diaminopropionate
medicine
-
nonvirulent Salmonella typhimurium PU011 can be used for the production of the enzyme to detoxify the neurotoxin 3-oxalyl and 2,3-dioxalyl diaminopropionate
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nagasawa, T.; Tanizawa, K.; Satoda, T.; Yamada, H.
Diaminopropionate ammonia-lyase from Salmonella typhimurium. Purification and characterization of the crystalline enzyme and sequence determination of the pyridoxal 5'-phosphate binding peptide
J. Biol. Chem.
263
958-964
1988
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