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Literature summary extracted from

  • Maggi, M.; Chiarelli, L.R.; Valentini, G.; Scotti, C.
    Engineering of Helicobacter pylori L-asparaginase: characterization of two functionally distinct groups of mutants (2015), PLoS ONE, 10, e0117025.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.1 expressed in Escherichia coli BL21(DE3) pLysS cells Helicobacter pylori

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 M121C mutants has nearly 2.5fold reduced catalytic activity compared to the wild type enzyme Helicobacter pylori
3.5.1.1 M121C/T169M the mutant has a preserved efficiency versus L-asparagine but is completely unable to carry out L-glutamine hydrolysis Helicobacter pylori
3.5.1.1 Q63E the mutant endows with a similar catalytic efficiency versus L-asparagine and halved glutaminase efficiency with respect to the wild type enzyme Helicobacter pylori
3.5.1.1 T169M mutants has nearly 4fold reduced catalytic activity compared to the wild type enzyme Helicobacter pylori
3.5.1.1 T16D inactive Helicobacter pylori
3.5.1.1 T95E inactive Helicobacter pylori

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.1 37000
-
 x * 37000, SDS-PAGE Helicobacter pylori

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.1 L-asparagine + H2O Helicobacter pylori strongly preferred substrate L-aspartate + NH3
-
 ?
3.5.1.1 L-asparagine + H2O Helicobacter pylori CCUG 17874 strongly preferred substrate L-aspartate + NH3
-
 ?
3.5.1.1 L-glutamine + H2O Helicobacter pylori
-
 L-glutamic acid + NH3
-
 ?
3.5.1.1 L-glutamine + H2O Helicobacter pylori CCUG 17874
-
 L-glutamic acid + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Helicobacter pylori I0ZIE0
-
-
3.5.1.1 Helicobacter pylori CCUG 17874 I0ZIE0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.1 HisTrap column chromatography and Superdex S200 gel filtration Helicobacter pylori

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.1 L-asparagine + H2O strongly preferred substrate Helicobacter pylori L-aspartate + NH3
-
 ?
3.5.1.1 L-asparagine + H2O strongly preferred substrate Helicobacter pylori CCUG 17874 L-aspartate + NH3
-
 ?
3.5.1.1 L-glutamine + H2O
-
 Helicobacter pylori L-glutamic acid + NH3
-
 ?
3.5.1.1 L-glutamine + H2O
-
 Helicobacter pylori CCUG 17874 L-glutamic acid + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.1 ? x * 37000, SDS-PAGE Helicobacter pylori

Synonyms

EC Number Synonyms Comment Organism
3.5.1.1 ASNase
-
 Helicobacter pylori
3.5.1.1 HPA
-
 Helicobacter pylori
3.5.1.1 L-ASNase
-
 Helicobacter pylori
3.5.1.1 type II L-asparaginase
-
 Helicobacter pylori

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.1 53
-
 the wild type enzyme shows 50% activity after 10 min incubation at 53°C Helicobacter pylori

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.1 4.83
-
 L-asparagine mutant enzyme M121C, at pH 7.5 and 37°C Helicobacter pylori
3.5.1.1 6.53
-
 L-asparagine mutant enzyme Q63E, at pH 7.5 and 37°C Helicobacter pylori
3.5.1.1 7.4
-
 L-asparagine mutant enzyme T169M, at pH 7.5 and 37°C Helicobacter pylori
3.5.1.1 13.95
-
 L-asparagine mutant enzyme M121C/T169M, at pH 7.5 and 37°C Helicobacter pylori
3.5.1.1 14.5
-
 L-glutamine mutant enzyme Q63E, at pH 7.5 and 37°C Helicobacter pylori
3.5.1.1 19.26
-
 L-asparagine wild type enzyme, at pH 7.5 and 37°C Helicobacter pylori
3.5.1.1 22.1
-
 L-glutamine wild type enzyme, at pH 7.5 and 37°C Helicobacter pylori