|PROSITE documentation PDOC00132|
Asparaginase (EC 18.104.22.168), glutaminase (EC 22.214.171.124) and glutaminase-asparaginase (EC 126.96.36.199) are aminohydrolases that catalyze the hydrolysis of asparagine (or glutamine) to aspartate (or glutamate) and ammonia .
Two conserved threonine residues have been shown [2,3] 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.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:
April 2006 / Pattern revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Tanaka S., Robinson E.A., Appella E., Miller M., Ammon H.L., Roberts J., Weber I.T., Wlodawer A.|
|Title||Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi.|
|Source||J. Biol. Chem. 263:8583-8591(1988).|
|2||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).|
|3||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).|