|PROSITE documentation PDOC00132 [for PROSITE entry PS00917]|
L-Asparaginases (EC 126.96.36.199) hydrolyze L-asparagine to L-aspartate and ammonia. Enzymes with asparaginase activity play an important role in the metabolism of all living organisms [1,2]. 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:
The asparaginase/glutaminase domain consists of two α/β subdomains that are connected by an extended but structured linker region. The larger N-terminal subdomain is characterized by an eight-stranded antiparallel mixed β-sheet. The smaller C-terminal subdomain contains a parallel β-sheet (see <PDB:2JK0>) .
Two conserved threonine residues have been shown [4,5] to play a catalytic role. One of them is located in the N-terminal extremity while the second is located at the end of the first third of the sequence. We used both conserved regions as signature patterns.
The profile we developed covers the entire asparaginase/glutaminase domain.Note:
Plant asparaginases and mammalian glutaminases do not belong to this family and are thus not detected by the above pattern.Expert(s) to contact by email:
October 2014 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Borek D. Jaskolski M.|
|Title||Sequence analysis of enzymes with asparaginase activity.|
|Source||Acta Biochim. Pol. 48:893-902(2001).|
|2||Authors||Michalska K. Jaskolski M.|
|Title||Structural aspects of L-asparaginases, their friends and relations.|
|Source||Acta Biochim. Pol. 53:627-640(2006).|
|3||Authors||Papageorgiou A.C. Posypanova G.A. Andersson C.S. Sokolov N.N. Krasotkina J.|
|Title||Structural and functional insights into Erwinia carotovora L-asparaginase.|
|Source||FEBS J. 275:4306-4316(2008).|
|4||Authors||Harms E. Wehner A. Aung H.P. Rohm K.H.|
|Title||A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis.|
|Source||FEBS Lett. 285:55-58(1991).|
|5||Authors||Miller M.M. Rao J.K.M. Wlodawer A. Gribskov M.R.|
|Title||A left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartate.|
|Source||FEBS Lett. 328:275-279(1993).|