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| 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) |
| Consensus pattern: |
[LIVM]-x-{L}-T-G(2)-T-[IV]-[AGS]
The second T is an active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
10. |
|
|
|
| Matching PDB structures:
1AGX 1DJO 1DJP 1HFJ ... [ALL] |
| ASN_GLN_ASE_2, PS00917; Asparaginase / glutaminase active site signature 2 (PATTERN) |
| Consensus pattern: |
[GA]-x-[LIVM]-x(2)-H-G-T-D-T-[LIVM]
The first T is an active site residue |
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
NONE. |
|
|
|
| Matching PDB structures:
1AGX 1DJO 1DJP 1HFJ ... [ALL] |
References:
| 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). |
| PubMed ID | 3379033 |
| 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). |
| PubMed ID | 1906013 |
| 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). |
| PubMed ID | 8348975 |
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