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Literature summary extracted from
- Role of asparaginase variable loop at the carboxyl terminal of the alpha subunit in the determination of substrate preference in plants (2012), Planta, 235, 1013-1022.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.5.1.1 | F162L | site-directed mutagenesis of ASPGB1, mutation of Phe162 immediately preceding the variable loop in K+-dependent ASPGB1 specifically affects catalytic activity with Asn, the mutant shows an 8.4fold decrease in Vmax value with Asn, whereas the Vmax with beta-Asp-His is similar to that of the wild-type enzyme | Arabidopsis thaliana |
| 3.5.1.1 | F162W | site-directed mutagenesis of ASPGB1, mutation of Phe162 immediately preceding the variable loop in K+-dependent ASPGB1 specifically affects catalytic activity with Asn, the mutant shows a 4fold decrease in Vmax value with Asn, whereas the Vmax with beta-Asp-His is similar to that of the wild-type enzyme | Arabidopsis thaliana |
| 3.5.1.1 | L163F | site-directed mutagenesis of ASPGA1, introduction of the more bulky residue in the ASPGA1 mutant only affects Km and Vmax values with beta-Asp-His and not those with Asn, with beta-Asp-His, the Vmax value of the L163F mutant is reduced by approximately fivefold and the Km value by twofold, compared to the wild-type enzyme | Arabidopsis thaliana |
| 3.5.1.1 | additional information | construction of chimeras of the variable loop at the C-terminal of the alpha subunit of ASPGA1 and ASPGB1, substrate specificities and kinetics compared to the wild-type enzyme, overview | Arabidopsis thaliana |
| 3.5.1.1 | N184A | site-directed mutagenesis of ASPGB1, the mutant shows a 3fold decrease in Vmax value with Asn as substrate | Arabidopsis thaliana |
| 3.5.1.1 | N184D | site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme | Arabidopsis thaliana |
| 3.5.1.1 | N184Q | site-directed mutagenesis of ASPGB1, the mutant shows a Vmax value with Asn as substrate that is similar or slightly higher than that of the wild-type ASPGB1 | Arabidopsis thaliana |
| 3.5.1.1 | R165T | site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme | Arabidopsis thaliana |
| 3.5.1.1 | S189A | site-directed mutagenesis of ASPGB1, the mutant shows a 3fold decrease in Vmax value with Asn as substrate | Arabidopsis thaliana |
| 3.5.1.1 | S189C | site-directed mutagenesis of ASPGB1, the mutant shows altered kinetics with substrate compared to the wild-type enzyme | Arabidopsis thaliana |
| 3.5.1.1 | S189T | site-directed mutagenesis of ASPGB1, the mutant shows a Vmax value with Asn as substrate that is similar or slightly higher than that of the wild-type ASPGB1 | Arabidopsis thaliana |
| 3.5.1.1 | T166R | site-directed mutagenesis of ASPGA1, introduction of the more bulky residue in the ASPGA1 mutant only affects Km and Vmax values with beta-Asp-His and not those with Asn | Arabidopsis thaliana |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.1 | aspartic acid | - |
Arabidopsis thaliana |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.5.1.1 | additional information | - |
additional information | kinetic parameters of wild-type and chimeric ASPGA1 and -B1, overview | Arabidopsis thaliana | |
| 3.5.1.1 | 2.38 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, wild-type ASPGB1 | Arabidopsis thaliana | |
| 3.5.1.1 | 2.9 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184A | Arabidopsis thaliana | |
| 3.5.1.1 | 3.13 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGA1 mutant T166R | Arabidopsis thaliana | |
| 3.5.1.1 | 3.25 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162L | Arabidopsis thaliana | |
| 3.5.1.1 | 3.25 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T | Arabidopsis thaliana | |
| 3.5.1.1 | 3.28 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q | Arabidopsis thaliana | |
| 3.5.1.1 | 3.56 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189C | Arabidopsis thaliana | |
| 3.5.1.1 | 3.9 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162W | Arabidopsis thaliana | |
| 3.5.1.1 | 4.11 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184D | Arabidopsis thaliana | |
| 3.5.1.1 | 4.15 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184D | Arabidopsis thaliana | |
| 3.5.1.1 | 4.23 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189A | Arabidopsis thaliana | |
| 3.5.1.1 | 4.53 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184A | Arabidopsis thaliana | |
| 3.5.1.1 | 4.72 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189C | Arabidopsis thaliana | |
| 3.5.1.1 | 4.91 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189A | Arabidopsis thaliana | |
| 3.5.1.1 | 5.12 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162W | Arabidopsis thaliana | |
| 3.5.1.1 | 5.56 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGB1 mutant F162L | Arabidopsis thaliana | |
| 3.5.1.1 | 5.62 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T | Arabidopsis thaliana | |
| 3.5.1.1 | 6.65 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGB1 mutant S189T | Arabidopsis thaliana | |
| 3.5.1.1 | 6.79 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F | Arabidopsis thaliana | |
| 3.5.1.1 | 6.83 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, wild-type ASPGB1 | Arabidopsis thaliana | |
| 3.5.1.1 | 10.5 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGB1 mutant N184Q | Arabidopsis thaliana | |
| 3.5.1.1 | 10.7 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGB1 mutant R165T | Arabidopsis thaliana | |
| 3.5.1.1 | 12.6 | - |
beta-Asp-His | pH 8.0, temperature not specified in the publication, wild-type ASPGA1 | Arabidopsis thaliana | |
| 3.5.1.1 | 12.7 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGA1 mutant L163F | Arabidopsis thaliana | |
| 3.5.1.1 | 14.3 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, ASPGA1 mutant T166R | Arabidopsis thaliana | |
| 3.5.1.1 | 14.7 | - |
L-asparagine | pH 8.0, temperature not specified in the publication, wild-type ASPGA1 | Arabidopsis thaliana | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.5.1.1 | K+ | potassium-independent asparaginase ASPGA1, and potassium-dependent asparaginase ASPGB1 | Arabidopsis thaliana | |
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 | Arabidopsis thaliana | - |
L-aspartate + NH3 | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.5.1.1 | Arabidopsis thaliana | - |
potassium-independent asparaginase ASPGA1, and potassium-dependent asparaginase ASPGB1 | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.5.1.1 | beta-Asp-His + H2O | substrate of ASPGA1 and ASPGB1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn | Arabidopsis thaliana | ? | - |
? | |
| 3.5.1.1 | L-asparagine + H2O | - |
Arabidopsis thaliana | L-aspartate + NH3 | - |
? | |
| 3.5.1.1 | L-asparagine + H2O | substrate of ASPGA1 and ASPGB1, but ASPGB1 has a 45fold higher specific activity with Asn as substrate than ASPGA1, ASPGA1 has a 4fold substrate preference for beta-Asp-His over Asn | Arabidopsis thaliana | L-aspartate + NH3 | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.5.1.1 | More | a divergent sequence between the two enzymes forms a variable loop at the C-terminal of the alpha subunit, the variable loop itself spans positions 169-182 of ASPGA1 and 168-194 of ASPGB1 | Arabidopsis thaliana |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.5.1.1 | ASPGA1 | - |
Arabidopsis thaliana |
| 3.5.1.1 | ASPGB1 | - |
Arabidopsis thaliana |
| 3.5.1.1 | potassium-dependent asparaginase | - |
Arabidopsis thaliana |
| 3.5.1.1 | potassium-independent asparaginase | - |
Arabidopsis thaliana |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.5.1.1 | 8 | - |
assay at | Arabidopsis thaliana |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.5.1.1 | additional information | a divergent sequence between the two enzymes forms a variable loop at the C-terminal of the alpha subunit, the asparaginase variable loop plays a role in the determination of substrate preference in plants. The variable loop itself spans positions 169-182 of ASPGA1 and 168-194 of ASPGB1, dynamic simulations and comparative protein structure modeling based on the crystal structure of Lupinus luteus LlA, PDB accession number 2GEZ, overview | Arabidopsis thaliana |
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