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InterPro: IPR000246 Peptidase T2, asparaginase 2

Protein matchesHelp
UniProtKB
Matches:
1028 proteins
AccessionHelp IPR000246 Peptidase_T2
TypeHelp Family
SignaturesHelp
GO Term annotationHelp
Function GO:0016787 hydrolase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

In the MEROPS database peptidases and peptidase homologues are grouped into clans and families. Clans are groups of families for which there is evidence of common ancestry based on a common structural fold:

  • Each clan is identified with two letters, the first representing the catalytic type of the families included in the clan (with the letter 'P' being used for a clan containing families of more than one of the catalytic types serine, threonine and cysteine). Some families cannot yet be assigned to clans, and when a formal assignment is required, such a family is described as belonging to clan A-, C-, M-, S-, T- or U-, according to the catalytic type. Some clans are divided into subclans because there is evidence of a very ancient divergence within the clan, for example MA(E), the gluzincins, and MA(M), the metzincins.
  • Peptidase families are grouped by their catalytic type, the first character representing the catalytic type: A, aspartic; C, cysteine; G, glutamic acid; M, metallo; S, serine; T, threonine; and U, unknown. The serine, threonine and cysteine peptidases utilise the amino acid as a nucleophile and form an acyl intermediate - these peptidases can also readily act as transferases. In the case of aspartic, glutamic and metallopeptidases, the nucleophile is an activated water molecule.

In many instances the structural protein fold that characterises the clan or family may have lost its catalytic activity, yet retain its function in protein recognition and binding.

Threonine peptidases are characterised by a threonine nucleophile at the N terminus of the mature enzyme. The threonine peptidases belong to clan PB or are unassigned, clan T-. The type example for this clan is the archaean proteasome beta component of Thermoplasma acidophilum.

This group of sequences have a signature that places them in MEROPS peptidase family T2 (clan PB(T)). The glycosylasparaginases (EC:3.5.1.26) are threonine peptidases. Also in this family is L-asparaginase (EC:3.5.1.1), which catalyses the following reaction:

L-asparagine + H2O = L-aspartate + NH3

Glycosylasparaginase catalyses:

N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H(2)O = N-acetyl-beta-glucosaminylamine + L-aspartate

cleaving the GlcNAc-Asn bond that links oligosaccharides to asparagine in N-linked glycoproteins. The enzyme is composed of two non-identical alpha/beta subunits joined by strong non-covalent forces and has one glycosylation site located in the alpha subunit [1] and plays a major role in the degradation of glycoproteins.

Structural linksHelp
Database linksHelp
Enzyme: EC:3
PANDIT: PF01112
Blocks: IPB000246
MEROPS: T2
Pfam Clan: CL0052.14

Taxonomic coverageHelp

Example proteinsHelp
O65268 Putative isoaspartyl peptidase/L-asparaginase 4

P20933 N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase

Q21697 Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase

Q64191 N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase

Q8MR45 Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase CG1827

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000246 Peptidase T2, asparaginase 2
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain

PublicationsHelp
1. Liu Y, Dunn GS, Aronson NN Jr.
Purification, biochemistry and molecular cloning of an insect glycosylasparaginase from Spodoptera frugiperda.
Glycobiology 6 527-36 1996 [PubMed: 8877373]
http://dx.doi.org/10.1093/glycob/6.5.527

Additional ReadingHelp
Xu Q, Buckley D, Guan C, Guo HC.
Structural insights into the mechanism of intramolecular proteolysis.
Cell 98 1999 651-61 [PubMed: 10490104]
http://dx.doi.org/10.1016/S0092-8674(00)80052-5
Prahl A, Pazgier M, Hejazi M, Lockau W, Lubkowski J.
Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 1173-6 [PubMed: 15159592]
http://dx.doi.org/10.1107/S0907444904003403
Guo HC, Xu Q, Buckley D, Guan C.
Crystal structures of Flavobacterium glycosylasparaginase. An N-terminal nucleophile hydrolase activated by intramolecular proteolysis.
J. Biol. Chem. 273 1998 20205-12 [PubMed: 9685368]
http://dx.doi.org/10.1074/jbc.273.32.20205
Qian X, Guan C, Guo HC.
A dual role for an aspartic acid in glycosylasparaginase autoproteolysis.
Structure 11 2003 997-1003 [PubMed: 12906830]
http://dx.doi.org/10.1016/S0969-2126(03)00150-3
Michalska K, Borek D, Hernandez-Santoyo A, Jaskolski M.
Crystal packing of plant-type L-asparaginase from Escherichia coli.
Acta Crystallogr. D Biol. Crystallogr. 64 2008 309-20 [PubMed: 18323626]
http://dx.doi.org/10.1107/S0907444907068072
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InterPro 23.1