Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.1.15
-
 Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15
-
 Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.1.15 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

EC Number Protein Variants Comment Organism
4.3.1.15 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
4.3.1.15 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
4.3.1.15 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
4.3.1.15 C299V mutation does not effect the activity Salmonella enterica subsp. enterica serovar Typhimurium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.15 0.02
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
4.3.1.15 0.03
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
4.3.1.15 0.04
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
4.3.1.15 0.11
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.3.1.15 0.13
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
4.3.1.15 0.17
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.3.1.15 0.24
-
 L-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15 0.28
-
 D-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.15 45220
-
 MALDI-TOF mass spectrometry Salmonella enterica subsp. enterica serovar Typhimurium

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.1.15
-
 Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.15 D-2,3-diaminopropanoate + H2O
-
 Escherichia coli pyruvate + 2 NH3
-
 ?
4.3.1.15 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
-
 ?
4.3.1.15 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
-
 ?
4.3.1.15 L-2,3-diaminopropanoate + H2O
-
 Escherichia coli pyruvate + 2 NH3
-
 ?
4.3.1.15 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
-
 ?
4.3.1.15 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

EC Number Subunits Comment Organism
4.3.1.15 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.1.15 37
-
 assay at Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15 37
-
 assay at Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.3.1.15 59
-
 Tm-value Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15 60
-
 Tm-value of the mutant enzyme C265S Escherichia coli
4.3.1.15 65
-
 Tm-value, wild-type enzyme Escherichia coli
4.3.1.15 68
-
 Tm-value of the mutant enzyme C291S Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.1.15 1.7
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
4.3.1.15 3.6
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
4.3.1.15 7.8
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
4.3.1.15 12.45
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
4.3.1.15 19
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.3.1.15 42.5
-
 D-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15 43.3
-
 L-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15 53.7
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.1.15 7.5
-
 assay at Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15 7.5
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.15 pyridoxal 5'-phosphate dependent on Escherichia coli
4.3.1.15 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]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.3.1.15 27.7
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
4.3.1.15 42.5
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C265S Escherichia coli
4.3.1.15 151.7
-
 D-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15 172.7
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.3.1.15 180.4
-
 L-2,3-diaminopropanoate pH 7.5, 37°C Salmonella enterica subsp. enterica serovar Typhimurium
4.3.1.15 315.9
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, wild-type enzyme Escherichia coli
4.3.1.15 390
-
 L-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli
4.3.1.15 415
-
 D-2,3-diaminopropanoate pH 7.5, 37°C, mutant enzyme C291S Escherichia coli