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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

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 M121C about 2.5fold reduced activtiy Helicobacter pylori
3.5.1.1 M121C/T169M mutant has a preserved efficiency vs L-asparagine but is completely unable to carry out L-glutamine hydrolysis. The mutant does not exert any cytotoxic effect on HL-60 cells Helicobacter pylori
3.5.1.1 Q63E mutant displays similar catalytic efficiency versus asparagine and halved glutaminase efficiency with respect to the wild type enzyme, is able to exert a cytotoxic effect comparable to, or higher than, the one of the wild type enzyme Helicobacter pylori
3.5.1.1 T169M about 4fold reduced catalytic activity Helicobacter pylori
3.5.1.1 T16D replacement of catalytic threonine, depletes the enzyme of its catalytic activities with L-asparagine and L-glutamine Helicobacter pylori
3.5.1.1 T95D replacement of catalytic threonine, depletes the enzyme of its catalytic activities with L-asparagine and L-glutamine Helicobacter pylori
3.5.1.2 M121C about 2.5fold reduced activtiy Helicobacter pylori
3.5.1.2 M121C/T169M mutant has a preserved efficiency vs L-asparagine but is completely unable to carry out L-glutamine hydrolysis. The mutant does not exert any cytotoxic effect on HL-60 cells Helicobacter pylori
3.5.1.2 Q63E mutant displays similar catalytic efficiency versus asparagine and halved glutaminase efficiency with respect to the wild type enzyme, is able to exert a cytotoxic effect comparable to, or higher than, the one of the wild type enzyme Helicobacter pylori
3.5.1.2 T169M about 4fold reduced catalytic activity Helicobacter pylori
3.5.1.2 T16D replacement of catalytic threonine, depletes the enzyme of its catalytic activities with L-asparagine and L-glutamine Helicobacter pylori
3.5.1.2 T95D replacement of catalytic threonine, depletes the enzyme of its catalytic activities with L-asparagine and L-glutamine Helicobacter pylori

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 0.1
-
L-asparagine mutant Q63E, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 0.23
-
L-asparagine mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 0.25
-
L-asparagine mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 0.25
-
L-asparagine mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 0.29
-
L-asparagine wild-type, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 46.4
-
L-glutamine wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 76.5
-
L-glutamine mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 0.1
-
L-asparagine mutant Q63E, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 0.23
-
L-asparagine mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 0.25
-
L-asparagine mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 0.25
-
L-asparagine mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 0.29
-
L-asparagine wild-type, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 46.4
-
L-glutamine wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 76.5
-
L-glutamine mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C Helicobacter pylori

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Helicobacter pylori A0A2X5A091
-
-
3.5.1.1 Helicobacter pylori ATCC 43504 A0A2X5A091
-
-
3.5.1.2 Helicobacter pylori A0A2X5A091
-
-
3.5.1.2 Helicobacter pylori ATCC 43504 A0A2X5A091
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.1 L-asparagine + H2O
-
Helicobacter pylori L-aspartate + NH3
-
?
3.5.1.1 L-asparagine + H2O
-
Helicobacter pylori ATCC 43504 L-aspartate + NH3
-
?
3.5.1.1 L-glutamine + H2O reaction of EC 3.5.1.2 Helicobacter pylori L-glutamate + NH3
-
?
3.5.1.1 L-glutamine + H2O reaction of EC 3.5.1.2 Helicobacter pylori ATCC 43504 L-glutamate + NH3
-
?
3.5.1.2 L-asparagine + H2O reaction of EC 3.5.1.1 Helicobacter pylori L-aspartate + NH3
-
?
3.5.1.2 L-asparagine + H2O reaction of EC 3.5.1.1 Helicobacter pylori ATCC 43504 L-aspartate + NH3
-
?
3.5.1.2 L-glutamine + H2O
-
Helicobacter pylori L-glutamate + NH3
-
?
3.5.1.2 L-glutamine + H2O
-
Helicobacter pylori ATCC 43504 L-glutamate + NH3
-
?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.1 AnsB
-
Helicobacter pylori
3.5.1.2 AnsB
-
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 2.1
-
L-glutamine wild-type, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 4.83
-
L-asparagine mutant M121C, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 6.53
-
L-asparagine mutant Q63E, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 7.4
-
L-asparagine mutant T169M, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 13.95
-
L-asparagine mutant M121C/T169M, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 14.5
-
L-glutamine mutant Q63E, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 19.2
-
L-asparagine wild-type, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 2.1
-
L-glutamine wild-type, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 4.83
-
L-asparagine mutant M121C, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 6.53
-
L-asparagine mutant Q63E, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 7.4
-
L-asparagine mutant T169M, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 13.95
-
L-asparagine mutant M121C/T169M, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 14.5
-
L-glutamine mutant Q63E, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 19.2
-
L-asparagine wild-type, pH 7.5, 37°C Helicobacter pylori

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.1.1 0.19
-
L-glutamine mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 0.47
-
L-glutamine wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 29.6
-
L-asparagine mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 30.2
-
L-asparagine mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 60.7
-
L-asparagine mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 65.3
-
L-asparagine mutant Q63E, pH 7.5, 37°C Helicobacter pylori
3.5.1.1 66.4
-
L-asparagine wild-type, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 0.19
-
L-glutamine mutant Q63E, cooperative kinetic toward L-Gln, Hill coefficient 2.3, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 0.47
-
L-glutamine wild-type, cooperative kinetic toward L-Gln, Hill coefficient 2.0, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 29.6
-
L-asparagine mutant T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.8, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 30.2
-
L-asparagine mutant M121C, cooperative kinetic toward L-Asn, Hill coefficient 1.5, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 60.7
-
L-asparagine mutant M121C/T169M, cooperative kinetic toward L-Asn, Hill coefficient 1.7, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 65.3
-
L-asparagine mutant Q63E, pH 7.5, 37°C Helicobacter pylori
3.5.1.2 66.4
-
L-asparagine wild-type, pH 7.5, 37°C Helicobacter pylori