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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,
more
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2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
2,3-diaminopropanoate + H2O
pyruvate + NH3
2-[5-amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide + H2O
?
-
-
-
-
?
D-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
-
-
-
?
D-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
D-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
D-serine + H2O
pyruvate + NH3
DL-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
-
-
-
?
DL-2,3-diaminopropanoate + H2O
pyruvate + NH3
L-2,3-diaminopropanoate + 2 H2O
pyruvate + 2 NH3
-
-
-
?
L-2,3-diaminopropanoate + H2O
pyruvate + 2 NH3
L-2,3-Diaminopropanoate + H2O
Pyruvate + 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
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 + 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
-
-
-
?
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
-
-
-
?
D-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
D-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
D-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
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-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
D-serine

pyruvate + NH3
-
-
-
?
D-serine
pyruvate + NH3
-
-
-
?
D-serine + H2O

pyruvate + NH3
-
-
-
?
D-serine + H2O
pyruvate + NH3
-
-
-
?
DL-2,3-diaminopropanoate + H2O

pyruvate + NH3
-
-
-
?
DL-2,3-diaminopropanoate + H2O
pyruvate + NH3
-
-
-
?
L-2,3-diaminopropanoate + H2O

pyruvate + 2 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-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
L-2,3-Diaminopropanoate + H2O
Pyruvate + NH3
-
-
-
?
L-serine

pyruvate + NH3
-
-
-
?
L-serine
pyruvate + NH3
-
-
-
?
L-serine
pyruvate + NH3
-
-
-
?
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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
0.03 - 12.9
D-2,3-diaminopropanoate
0.014 - 0.52
DL-2,3-diaminopropanoate
0.02 - 11.5
L-2,3-diaminopropanoate
0.284
L-cysteine
pH 7.4, 30°C, mutant T385D sDAPL
0.741
2,3-Diaminopropionate

-
recombinant enzyme, 0.683 using Lathyrus sativus seed extracts as substrate
0.74
2,3-Diaminopropionate
-
wild type enzyme, 0.680 using Lathyrus sativus seed extracts as substrate
12.9
D-2,3-diaminopropanoate

-
mutant D189N, pH and temperature not specified in the publication
0.28
D-2,3-diaminopropanoate
pH 7.5, 37°C
0.27
D-2,3-diaminopropanoate
-
-
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
0.17
D-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
0.346
D-2,3-diaminopropanoate
pH 7.4, 30°C, mutant D125S sDAPL
0.13
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
0.05
D-2,3-diaminopropanoate
wild-type, pH and temperature not specified in the publication
0.03
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
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
0.33
D-serine
pH 7.4, 30°C, sDAPL
0.72
D-serine
-
pH 7.5, 37°C
0.285
D-serine
-
pH 7.5, 37°C
0.279
DL-2,3-diaminopropanoate

pH 7.4, 30°C, untagged sDAPL
0.52
DL-2,3-diaminopropanoate
pH 7.4, 30°C, mutant T385D sDAPL
0.43
DL-2,3-diaminopropanoate
pH 7.4, 30°C, mutant C299V sDAPL
0.382
DL-2,3-diaminopropanoate
pH 7.4, 30°C, mutant T385S sDAPL
0.17
DL-2,3-diaminopropanoate
-
pH 7.5, 37°C
0.33
DL-2,3-diaminopropanoate
-
pH 7.5, 37°C
0.3
DL-2,3-diaminopropanoate
pH 7.4, 30°C, sDAPL
0.014
DL-2,3-diaminopropanoate
pH 7.4, 30°C, mutant C271V sDAPL
11.5
L-2,3-diaminopropanoate

mutant D189N, pH and temperature not specified in the publication
1
L-2,3-diaminopropanoate
-
-
11.5
L-2,3-diaminopropanoate
-
mutant D189N, pH and temperature not specified in the publication
0.03
L-2,3-diaminopropanoate
wild-type, pH and temperature not specified in the publication
0.04
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
0.02
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
0.11
L-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
0.57
L-2,3-diaminopropanoate
mutant D120N, pH and temperature not specified in the publication
0.11
L-2,3-diaminopropanoate
-
pH 7.5, 37°C, wild-type enzyme
0.412
L-2,3-diaminopropanoate
pH 7.4, 30°C, mutant D125E sDAPL
0.378
L-2,3-diaminopropanoate
pH 7.4, 30°C, mutant D194S sDAPL
0.12
L-2,3-diaminopropanoate
-
-
0.24
L-2,3-diaminopropanoate
pH 7.5, 37°C
0.3
L-2,3-diaminopropanoate
pH 7.4, 30°C, mutant D125S sDAPL
0.24
L-2,3-diaminopropanoate
-
pH 7.5, 37°C
0.246
L-2,3-diaminopropanoate
pH 7.4, 30°C, sDAPL
6.3
L-serine

-
pH 7.5, 37°C
7.33
L-serine
-
pH 7.5, 37°C
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0.35 - 375.8
D-2,3-diaminopropanoate
34 - 69.17
DL-2,3-diaminopropanoate
0.18 - 43.3
L-2,3-diaminopropanoate
2
L-cysteine
pH 7.4, 30°C, mutant T385D sDAPL
375.8
D-2,3-diaminopropanoate

pH 7.4, 30°C, 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
12.45
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
7.83
D-2,3-diaminopropanoate
pH 7.4, 30°C, mutant D125S sDAPL
44.58
D-2,3-diaminopropanoate
wild-type, pH and temperature not specified in the publication
3.6
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
53.7
D-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
0.35
D-2,3-diaminopropanoate
mutant D189N, pH and temperature not specified in the publication
5.17
D-serine

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
51.67
DL-2,3-diaminopropanoate

pH 7.4, 30°C, mutant T385S sDAPL
42
DL-2,3-diaminopropanoate
pH 7.4, 30°C, mutant T385D sDAPL
34
DL-2,3-diaminopropanoate
pH 7.4, 30°C, mutant C271V sDAPL
69.17
DL-2,3-diaminopropanoate
pH 7.4, 30°C, untagged sDAPL
60.17
DL-2,3-diaminopropanoate
pH 7.4, 30°C, sDAPL
57
DL-2,3-diaminopropanoate
pH 7.4, 30°C, mutant C299V sDAPL
42.83
L-2,3-diaminopropanoate

pH 7.4, 30°C, sDAPL
43.3
L-2,3-diaminopropanoate
pH 7.5, 37°C
20.83
L-2,3-diaminopropanoate
pH 7.4, 30°C, mutant D125E sDAPL
37.33
L-2,3-diaminopropanoate
pH 7.4, 30°C, mutant D125S sDAPL
24.6
L-2,3-diaminopropanoate
wild-type, pH and temperature not specified in the publication
0.18
L-2,3-diaminopropanoate
mutant D189N, pH and temperature not specified in the publication
19
L-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
7.8
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
3.05
L-2,3-diaminopropanoate
mutant D120N, pH and temperature not specified in the publication
2.67
L-2,3-diaminopropanoate
pH 7.4, 30°C, mutant D194S sDAPL
1.7
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
0.18
L-2,3-diaminopropanoate
-
mutant D189N, pH and temperature not specified in the publication
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0.0266 - 890
D-2,3-diaminopropanoate
0.001 - 820
L-2,3-diaminopropanoate
890
D-2,3-diaminopropanoate

-
wild-type, pH and temperature not specified in the publication
315.9
D-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
415
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
151.7
D-2,3-diaminopropanoate
pH 7.5, 37°C
415
D-2,3-diaminopropanoate
-
pH 7.5, 37°C, mutant enzyme C291S
27.7
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
890
D-2,3-diaminopropanoate
wild-type, pH and temperature not specified in the publication
0.0266
D-2,3-diaminopropanoate
mutant D189N, pH and temperature not specified in the publication
820
L-2,3-diaminopropanoate

wild-type, pH and temperature not specified in the publication
390
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
172.7
L-2,3-diaminopropanoate
-
pH 7.5, 37°C, wild-type enzyme
180.4
L-2,3-diaminopropanoate
pH 7.5, 37°C
0.001
L-2,3-diaminopropanoate
mutant D189N, pH and temperature not specified in the publication
172.7
L-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
42.5
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
5.35
L-2,3-diaminopropanoate
mutant D120N, pH and temperature not specified in the publication
0.001
L-2,3-diaminopropanoate
-
mutant D189N, pH and temperature not specified in the publication
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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
D189N
Km (D-DAP) and (L-DAP) increased compared to wild-type, kcat decreased
D120N
mutant shows no reaction with D-DAP, Km (L-DAP) increased compared to wild-type, kcat decreased
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
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
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
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
D125S
kcat value in mutant is reduced by 5.4fold for D-DAP compared to wild-type
D125E
mutant does not show any activity with D-DAP at all
C299V
-
mutation does not effect the activity
-
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
C299V
kcat and Km for DL-DAP are similar 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
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
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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
Devosia riboflavina, Pseudomonas fluorescens, Salmonella enterica subsp. enterica serovar Typhimurium, Streptomyces ruber
brenda
Rao, D.R.; Hariharan, K.; Vijayalakshmi, K.R.
A specific enzymatic procedure for the determination of neurotoxic components (derivatives of L-alpha,beta-diaminopropionic acid) in Lathyrus sativus
J. Agric. Food Chem.
22
1147-1149
1974
Pseudomonas sp.
-
brenda
Vijayalakshmi, K.R.; Rao, D.R.; Rao, M.R.R.
Studies on a 2,3-diaminopropionate:ammonia-lyase from a pseudomonad
Hoppe-Seyler's Z. Physiol. Chem.
356
193-201
1975
Pseudomonas sp.
brenda
Rajaram, V.; Rajaganapathi, J.; Khan, F.; Savithri, H.S.; Murthy, M.R.
Crystallization and preliminary X-ray diffraction studies on recombinant diaminopropionate ammonia lyase from Escherichia coli
Acta Crystallogr. Sect. D
59
1668-1669
2003
Escherichia coli
brenda
Khan, F.; Jala, V.R.; Rao, N.A.; Savithri, H.S.
Characterization of recombinant diaminopropionate ammonia-lyase from Escherichia coli and Salmonella typhimurium
Biochem. Biophys. Res. Commun.
306
1083-1088
2003
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Rupesh, K.R.; PremKumar, P.L.; Kumar, V.V.S.; Jayachandran, S.S.
Production of diamino propionic acid ammonia lyase by a new strain of Salmonella typhimurium PU011
BMC Microbiol.
2
5
2002
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Rupesh, K.R.; Padma, K.R.; Saravanan, P.; Jayachandran, S.
Cloning, expression, and sequence analysis of diaminopropionate ammonia lyase gene from a nonvirulent Salmonella typhimurium PU011
Appl. Biochem. Biotechnol.
141
161-174
2007
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium PU011
brenda
Kalyani, J.N.; Ramachandra, N.; Kachroo, A.H.; Mahadevan, S.; Savithri, H.S.
Functional analysis of the genes encoding diaminopropionate ammonia lyase in Escherichia coli and Salmonella enterica serovar Typhimurium
J. Bacteriol.
194
5604-5612
2012
Escherichia coli (P66899), Escherichia coli, Salmonella enterica (P40817), Salmonella enterica subsp. enterica serovar Typhimurium (P40817)
brenda
Bisht, S.; Rajaram, V.; Bharath, S.R.; Kalyani, J.N.; Khan, F.; Rao, A.N.; Savithri, H.S.; Murthy, M.R.
Crystal structure of Escherichia coli diaminopropionate ammonia-lyase reveals mechanism of enzyme activation and catalysis
J. Biol. Chem.
287
20369-20381
2012
Escherichia coli (P66899), Escherichia coli
brenda
Deka, G.; Bisht, S.; Savithri, H.S.; Murthy, M.R.N.
Comparative structural and enzymatic studies on Salmonella typhimurium diaminopropionate ammonia lyase reveal its unique features
J. Struct. Biol.
202
118-128
2018
Escherichia coli (P66899), Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium (P40817), Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 (P40817)
brenda
Ernst, D.C.; Anderson, M.E.; Downs, D.M.
L-2,3-diaminopropionate generates diverse metabolic stresses in Salmonella enterica
Mol. Microbiol.
101
210-223
2016
Salmonella enterica (P40817), Salmonella enterica, Salmonella enterica DM14828 (P40817)
brenda