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Literature summary extracted from

  • Wang, Y.; Cao, X.; Feng, Y.; Xue, S.
    Environment-induced conformational and functional changes of L-2-haloacid dehalogenase (2016), J. Biosci. Bioeng., 121, 491-496 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.8.1.2 expression in Escherichia coli BL21 Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.8.1.2 Ag+ 1 mM, no activity is retained Pseudomonas putida
3.8.1.2 Ca2+ 1 mM, induced 3.4% decrease in alpha-helix, 4.4% increase in beta-sheet, respectively, with less than 25% activity loss in activity Pseudomonas putida
3.8.1.2 Cu2+ 1 mM, induces the transition of alpha-helix to beta-sheet and random coil at the same time with more than half of the enzymatic activity loss Pseudomonas putida
3.8.1.2 Hg2+ 1 mM, no activity is retained Pseudomonas putida
3.8.1.2 additional information little effects on alpha-helix and HadL AJ1 activity are observed with the presence of 1 mM Co2+ Pseudomonas putida
3.8.1.2 Zn2+ 1 mM, induced 5.1% decrease in alpha-helix, 5.4% increase in beta-sheet, respectively, with less than 25% activity loss in activity Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.8.1.2 53800
-
 gel filtration Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
3.8.1.2 Pseudomonas putida Q52087
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.8.1.2
-
 Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.8.1.2 (S)-2-chloropropionate + H2O
-
 Pseudomonas putida (R)-2-hydroxypropionic acid + chloride
-
 ?
3.8.1.2 additional information the alpha-helical structure of the enzyme plays a significant role during catalysis, while beta-sheet formation is a functional disadvantage. Analysis of environment-induced conformational and functional changes of 2-haloacid dehalogenase is informative for understanding the molecular basis of its stability and the design of the enzyme for future biotechnological applications in conjunction with its biochemical properties Pseudomonas putida ?
-
-

Subunits

EC Number Subunits Comment Organism
3.8.1.2 homodimer 2 * 26800, SDS-PAGE Pseudomonas putida

Synonyms

EC Number Synonyms Comment Organism
3.8.1.2 HadL AJ1
-
 Pseudomonas putida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.8.1.2 50
-
-
 Pseudomonas putida

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.8.1.2 40 60 40°C: about 40% of maximal activity, 60°C: about 70% of maximal activity Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.8.1.2 10
-
-
 Pseudomonas putida

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.8.1.2 9 11 pH 9.0: about 60% of maximal activity, pH 11.0: about 60% of maximal activity Pseudomonas putida

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.8.1.2 7 8 24 h, structural and functional stability Pseudomonas putida