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Synonyms
dapal, ecdapal, diaminopropionate ammonia-lyase, sdapal, diaminopropionate ammonia lyase, stm1002, alpha,beta-diaminopropionate ammonia-lyase, 2,3-diaminopropionate:ammonia-lyase,
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
0.74
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
0.03
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
0.05
D-2,3-diaminopropanoate
wild-type, pH and temperature not specified in the publication
0.13
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
0.17
D-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
0.27
D-2,3-diaminopropanoate
-
-
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
0.285
D-serine
-
pH 7.5, 37°C
0.33
D-serine
pH 7.4, 30°C, sDAPL
0.375
D-serine
pH 7.4, 30°C, mutant T385S sDAPL
0.6
D-serine
pH 7.4, 30°C, mutant T385D sDAPL
0.72
D-serine
-
pH 7.5, 37°C
0.014
DL-2,3-diaminopropanoate
pH 7.4, 30°C, mutant C271V sDAPL
0.17
DL-2,3-diaminopropanoate
-
pH 7.5, 37°C
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
0.02
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
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
0.11
L-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
0.12
L-2,3-diaminopropanoate
-
-
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
1
L-2,3-diaminopropanoate
-
-
11.5
L-2,3-diaminopropanoate
mutant D189N, pH and temperature not specified in the publication
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
0.35
D-2,3-diaminopropanoate
mutant D189N, pH and temperature not specified in the publication
3.6
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
7.83
D-2,3-diaminopropanoate
pH 7.4, 30°C, mutant D125S sDAPL
12.45
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
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
53.7
D-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
375.8
D-2,3-diaminopropanoate
pH 7.4, 30°C, sDAPL
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
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
1.7
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
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
7.8
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
19
L-2,3-diaminopropanoate
pH 7.5, 37°C, wild-type enzyme
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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0.0266 - 890
D-2,3-diaminopropanoate
0.001 - 820
L-2,3-diaminopropanoate
0.0266
D-2,3-diaminopropanoate
mutant D189N, pH and temperature not specified in the publication
27.7
D-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
151.7
D-2,3-diaminopropanoate
pH 7.5, 37°C
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
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
42.5
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C265S
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
390
L-2,3-diaminopropanoate
pH 7.5, 37°C, mutant enzyme C291S
820
L-2,3-diaminopropanoate
wild-type, 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
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
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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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
Pseudomonas fluorescens, Devosia riboflavina, 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
Salmonella enterica (P40817), Salmonella enterica subsp. enterica serovar Typhimurium (P40817), Escherichia coli (P66899), Escherichia coli
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
Salmonella enterica subsp. enterica serovar Typhimurium (P40817), Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli (P66899), Escherichia coli, 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