Information on EC 4.3.1.15 - Diaminopropionate ammonia-lyase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.3.1.15
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RECOMMENDED NAME
GeneOntology No.
Diaminopropionate ammonia-lyase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,3-diaminopropanoate + H2O = pyruvate + 2 NH3
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination of NH3
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.
CAS REGISTRY NUMBER
COMMENTARY hide
51901-19-0
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-diaminopropanoate + H2O
pyruvate + NH3
show the reaction diagram
D-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
show the reaction diagram
-
-
-
?
D-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
show the reaction diagram
D-serine
pyruvate + NH3
show the reaction diagram
D-serine + H2O
pyruvate + NH3
show the reaction diagram
DL-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
show the reaction diagram
-
-
-
?
DL-2,3-diaminopropanoate + H2O
pyruvate + NH3
show the reaction diagram
L-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
show the reaction diagram
-
-
-
?
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
show the reaction diagram
L-serine
pyruvate + NH3
show the reaction diagram
additional information
?
-
-
the enzyme is induced only by L-2,3-diaminopropionate or D-2,3-diaminopropanoate
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-
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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
additional information
?
-
-
the enzyme is induced only by L-2,3-diaminopropionate or D-2,3-diaminopropanoate
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
addition of increasing concentrations (higher than 10 mM) enhances the activity by 10fold
NaCl
addition of increasing concentrations enhances the activity by 2fold
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Iodosylbenzoate
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-
hydroxylamine
NaHSO3
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Semicarbazide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.74 - 0.741
2,3-Diaminopropionate
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
0.05 - 12.9
D-2,3-Diaminopropanoate
0.285 - 0.72
D-serine
0.014 - 0.52
DL-2,3-diaminopropanoate
0.03 - 11.5
L-2,3-diaminopropanoate
0.284
L-cysteine
pH 7.4, 30°C, mutant T385D sDAPL
6.3 - 7.33
L-serine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.35 - 375.8
D-2,3-Diaminopropanoate
5.17 - 34.17
D-serine
34 - 69.17
DL-2,3-diaminopropanoate
0.18 - 42.83
L-2,3-diaminopropanoate
2
L-cysteine
Salmonella enterica subsp. enterica serovar Typhimurium
P40817
pH 7.4, 30°C, mutant T385D sDAPL
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0266 - 890
D-2,3-Diaminopropanoate
45432
0.001 - 820
L-2,3-diaminopropanoate
20756
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.21
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pH 7.5, 37°C, apoenzyme
0.346
-
of the recombinant enzyme in crude extracts
0.351
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of the wild type enzyme in crude extracts
90.3
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pH 7.5, 37°C, holoenzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
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drastic reduction in activity above pH 11, below pH 6
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43300
-
calculated from cDNA
45000
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2 * 45000, SDS-PAGE
80000
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gel filtration
84000
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gel filtration
89000
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equilibrium ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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pH 7.0, 10 min, 50% loss of activity
60
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pH 7.0, 10 min, 90% loss of activity
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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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
low expression of ygeX gene is shown by RT-PCR
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D120N
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mutant shows no reaction with D-DAP, Km (L-DAP) increased compared to wild-type, kcat decreased
D189N
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Km (D-DAP) and (L-DAP) increased compared to wild-type, kcat decreased
D120N
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mutant shows no reaction with D-DAP, Km (L-DAP) increased compared to wild-type, kcat decreased
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D189N
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Km (D-DAP) and (L-DAP) increased compared to wild-type, kcat decreased
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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
C299V
kcat and Km for DL-DAP are similar to wild-type
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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
about 60% reconstitution of apoenzyme by addition of pyridoxal 5'-phosphate
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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a specific enzymatic procedure for the determination of neurotoxic components, derivatives of L-2,3-diaminopropanoate with diaminopropanonate ammonia-lyase
medicine
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