PROSITE documentation PDOC00132

Asparaginase / glutaminase active sites signatures




Description

Asparaginase (EC 3.5.1.1), glutaminase (EC 3.5.1.2) and glutaminase-asparaginase (EC 3.5.1.38) 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.

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:

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)


References

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



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)