| Fam ? Class - Clan - Family | Alt ? Alternative historical name / classification | AN ? UniProt accession number | Name ? UniProt entry name, only given here for Swiss-Prot entries | EC | Organism | Cell-Loc | AAs | Structure | PDB | Km i for Asn [mM] | Vmax i for Asn [μmol/min/mg] | Kcat i for Asn [s-1] | |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 1-5-14 | CpAI | H0W0T5 | 3.5.1.1 | Cavia porcellus | - | 565 | Homo tetramer i Additional ankrytin repeats. | 4R8L PDBs | 0.057 | - | 38.6 | ||
| 1-5-14 | hAI | Q86U10 | LPP60_HUMAN | 3.1.1.5 3.5.1.1 3.1.1.47 | Homo sapiens | - | 573 | Monomer i At assay conditions, substrate-inducing effect on the oligomeric state | - | 11.5 i S0.5, alloseric enzyme | - | 6.7 |
| Fam ? Class - Clan - Family | Alt ? Alternative historical name / classification | AN ? UniProt accession number | Name ? UniProt entry name, only given here for Swiss-Prot entries | EC | Organism | Cell-Loc | AAs | Structure | PDB | Km i for Asn [mM] | Vmax i for Asn [μmol/min/mg] | Kcat i for Asn [s-1] | |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 1-5-14 | - | Q9U518 | ASPG_DIRIM | 3.5.1.1 | Dirofilaria immitis | - | 590 | - | - | - | - | - | |
| 1-5-14 | hAI | Q86U10 | LPP60_HUMAN | 3.1.1.5 3.5.1.1 3.1.1.47 | Homo sapiens | - | 573 | Monomer i At assay conditions, substrate-inducing effect on the oligomeric state. Has additional ankyrin repeats. | - | 11.5 i S0.5, alloseric enzyme | - | 6.7 | |
| 1-5-14 | - | A0JNU3 | LPP60_MOUSE | 3.1.1.5 3.5.1.1 3.1.1.47 | Mus musculus | - | 564 | - | - | - | - | - | |
| 1-5-14 | - | O88202 | LPP60_RAT | 3.1.1.5 3.5.1.1 3.1.1.47 | Rattus norvegicus | - | 564 | - | - | - | - | - |
Clan 5 is the clan that holds many of the historical bacterial "type I" L-asparaginases as well as L-asparaginases from fungi and metazoans, including humans.
Family 14 contains the metazoan L-asparaginases, many of these are named 60 kDa lysophospholipase (LPP60) due to homology to the Rattus norvegicus LPP60 (O88202), also found in this family, which in addition to L-asparaginase activity presents lysophospholipase, transacetylase and acetylhydrolase activities. Most of the sequences have ankyrin repeats, but their function is unknown in this case, and an additional alpha helix in the N-terminal L-asparaginase domain, when compared to sequences in other families. The Cavia porcellus CpAI (H0W0T5) presents as a tetramer (dimer of two dimers) and has a surprisingly low KM when using L-asparagine as a substrate, comparable to that of ErAII, and undetectable L-glutaminase activity. In contrast, the human homolog; Homo sapiens HsAI (Q86U10), is an allosteric enzyme with low affinity to L-asparagine.
