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Literature summary for 4.3.1.15 extracted from

  • 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 (2018), J. Struct. Biol., 202, 118-128 .
    View publication on PubMed
Search for more literature for 4.3.1.15

Cloned(Commentary)

Cloned (Comment) Organism
-
 Salmonella enterica subsp. enterica serovar Typhimurium
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
microbatch method, the three-dimensional X-ray crystal structure of the enzyme is determined at 2.5 A resolution Salmonella enterica subsp. enterica serovar Typhimurium

Protein Variants

Protein Variants Comment Organism
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 Escherichia coli
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 Salmonella enterica subsp. enterica serovar Typhimurium
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 Escherichia coli
C299V mutation does not effect the activity Salmonella enterica subsp. enterica serovar Typhimurium

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
0.03
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
0.04
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
0.11
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
0.13
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
0.17
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
0.24
-
 L-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
0.28
-
 D-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

Metals/Ions Comment Organism Structure
K+ higher activity of the enzyme in the presence of K+ when compared to Na+ Salmonella enterica subsp. enterica serovar Typhimurium
Na+ higher activity of the enzyme in the presence of K+ when compared to Na+ Salmonella enterica subsp. enterica serovar Typhimurium

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
45220
-
 MALDI-TOF mass spectrometry Salmonella enterica subsp. enterica serovar Typhimurium

Organism

Organism UniProt Comment Textmining
Escherichia coli P66899
-
-
Salmonella enterica subsp. enterica serovar Typhimurium P40817
-
-
Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 P40817
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Salmonella enterica subsp. enterica serovar Typhimurium
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-2,3-diaminopropanoate + H2O
-
 Escherichia coli pyruvate + 2 NH3
-
 ?
D-2,3-diaminopropanoate + H2O 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 Salmonella enterica subsp. enterica serovar Typhimurium pyruvate + 2 NH3
-
 ?
D-2,3-diaminopropanoate + H2O 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 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 pyruvate + 2 NH3
-
 ?
L-2,3-diaminopropanoate + H2O
-
 Escherichia coli pyruvate + 2 NH3
-
 ?
L-2,3-diaminopropanoate + H2O 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 Salmonella enterica subsp. enterica serovar Typhimurium pyruvate + 2 NH3
-
 ?
L-2,3-diaminopropanoate + H2O 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 Salmonella enterica subsp. enterica serovar Typhimurium ATCC 700720 pyruvate + 2 NH3
-
 ?

Subunits

Subunits Comment Organism
dimer the enzyme is active as a dimer, it has a tendency to form a higher oligomer at high concentrations Salmonella enterica subsp. enterica serovar Typhimurium

Synonyms

Synonyms Comment Organism
DAPAL
-
 Salmonella enterica subsp. enterica serovar Typhimurium
DAPAL
-
 Escherichia coli
diaminopropionate ammonia lyase
-
 Salmonella enterica subsp. enterica serovar Typhimurium
diaminopropionate ammonia lyase
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Salmonella enterica subsp. enterica serovar Typhimurium
37
-
 assay at Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
59
-
 Tm-value Salmonella enterica subsp. enterica serovar Typhimurium
60
-
 Tm-value of the mutant enzyme C265S Escherichia coli
65
-
 Tm-value, wild-type enzyme Escherichia coli
68
-
 Tm-value of the mutant enzyme C291S Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.7
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
3.6
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
7.8
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
12.45
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
19
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
42.5
-
 D-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
43.3
-
 L-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
53.7
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Salmonella enterica subsp. enterica serovar Typhimurium
7.5
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Escherichia coli
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 Salmonella enterica subsp. enterica serovar Typhimurium

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
27.7
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
42.5
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
151.7
-
 D-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
172.7
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
180.4
-
 L-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
315.9
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
390
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
415
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli