ExplorEnz: EC 3.5.1.119

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3.5.1.119

Accepted name:

Pup amidohydrolase

Reaction:

[prokaryotic ubiquitin-like protein]-L-glutamine + H₂O = [prokaryotic ubiquitin-like protein]-L-glutamate + NH₃

Other name(s):

dop (gene name); Pup deamidase; depupylase/deamidase; DPUP; depupylase

Systematic name:

[prokaryotic ubiquitin-like protein]-L-glutamine amidohydrolase

Comments:

The enzyme has been characterized from the bacterium Mycobacterium tuberculosis. It catalyses the hydrolysis of the amido group of the C-terminal glutamine of prokaryotic ubiquitin-like protein (Pup), thus activating it for ligation to target proteins, a process catalysed by EC 6.3.1.19, prokaryotic ubiquitin-like protein ligase. The reaction requires ATP as cofactor but not its hydrolysis. The enzyme also catalyses the hydrolytic cleavage of the bond formed by the ligase, between an ε-amino group of a lysine residue of the target protein and the γ-carboxylate of the C-terminal glutamate of the prokaryotic ubiquitin-like protein.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Striebel, F., Imkamp, F., Sutter, M., Steiner, M., Mamedov, A. and Weber-Ban, E. Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat. Struct. Mol. Biol. 16 (2009) 647–651. [DOI] [PMID: 19448618]
2.	Burns, K.E., Cerda-Maira, F.A., Wang, T., Li, H., Bishai, W.R. and Darwin, K.H. "Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates. Mol. Cell 39 (2010) 821–827. [DOI] [PMID: 20705495]
3.	Striebel, F., Imkamp, F., Özcelik, D. and Weber-Ban, E. Pupylation as a signal for proteasomal degradation in bacteria. Biochim. Biophys. Acta 1843 (2014) 103–113. [DOI] [PMID: 23557784]

[EC 3.5.1.119 created 2015]