PROSITE documentation PDOC00132

Asparaginase / glutaminase active sites signatures


Asparaginase (EC, glutaminase (EC and glutaminase-asparaginase (EC are aminohydrolases that catalyze the hydrolysis of asparagine (or glutamine) to aspartate (or glutamate) and ammonia [1].

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.


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:

Gribskov M.

Last update:

April 2006 / Pattern revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

ASN_GLN_ASE_1, PS00144; Asparaginase / glutaminase active site signature 1  (PATTERN)

ASN_GLN_ASE_2, PS00917; Asparaginase / glutaminase active site signature 2  (PATTERN)


1AuthorsTanaka S., Robinson E.A., Appella E., Miller M., Ammon H.L., Roberts J., Weber I.T., Wlodawer A.
TitleStructures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi.
SourceJ. Biol. Chem. 263:8583-8591(1988).
PubMed ID3379033

2AuthorsHarms E., Wehner A., Aung H.P., Rohm K.H.
TitleA catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis.
SourceFEBS Lett. 285:55-58(1991).
PubMed ID1906013

3AuthorsMiller M.M., Rao J.K.M., Wlodawer A., Gribskov M.R.
TitleA left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartate.
SourceFEBS Lett. 328:275-279(1993).
PubMed ID8348975

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