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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.

Plant asparaginases and mammalian glutaminases do not belong to this family and are thus not detected by the above pattern.

Gribskov M.

April 2006 / Pattern revised.

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.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00144 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00144 • Scan Swiss-Prot/TrEMBL entries against PS00144 • view ligand binding statistics

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.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00917 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00917 • Scan Swiss-Prot/TrEMBL entries against PS00917 • view ligand binding statistics

Matching PDB structures: 1AGX 1DJO 1DJP 1HFJ ... [ALL]

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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