| Primary Identifier | IPR036152 | Type | Homologous_superfamily |
| Short Name | Asp/glu_Ase-like_sf |
| description | L-Asparaginases () hydrolyze L-asparagine to L-aspartate and ammonia. Enzymes with asparaginase activity play an important role in the metabolism of all living organisms [, ]. Enzymes capable of converting L-asparagine to L-aspartate can be classified as bacterial-type or plant-type L-asparaginase. Bacterial-type L-asparaginase are further divided into subtypes I and II, defined by their intra-/extra-cellular localization, substrate affinity, and oligomeric form. Homologous bacterial-type L-asparaginase are found in all kingdoms of life. Furthermore, bacterial-type L-asparaginase are related to other enzymes, including:Bacterial L-glutaminase-asparaginase () [].Archaeal GatD subunit of Glu-tRNA amidotransferase (Glu-AdT) [].Mammalian lysophospholipase (), which is believed to play a majorrole in the hydrolytic degradation of lysophosphatidylcholine [].The asparaginase/glutaminase structure consists of two non-similar alpha/beta domains, each domain has three layers (alpha/beta/alpha). The first domain has mixed β-sheet of six strands with strand 6 antiparallel to the rest and left-handed crossover connection between strands 4 and 5. The second domain has parallel β-sheet of four strands. |
