ExplorEnz: EC 3.4.11.27

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3.4.11.27

Accepted name:

archaeal arginyl aminopeptidase

Reaction:

Release of an N-terminal L-arginine from a protein with only minimal activity against other amino acids. L-Arg-7-amido-4-methylcoumarin is the best artificial substrate.

Other name(s):

arginyl aminopeptidase PH1704; PH1704; PfpI peptidase; C56.001 (Merops Identifier)

Comments:

The enzyme from the archaeon Pyrococcus horikoshii OT3 is thermostable. In that enzyme Cys¹⁰⁰ is the nucleophile responsible for the proteolytic activity, while Tyr¹²⁰ regulates the catalytic conformation of Cys¹⁰⁰ through a hydrogen bond, thereby affecting enzyme activity. The activity with L-Arginine is 90-300 times higher than with other N-terminal amino acids. The enzyme shows low endopeptidase activity.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Du, X., Choi, I.G., Kim, R., Wang, W., Jancarik, J., Yokota, H. and Kim, S.H. Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-Å resolution. Proc. Natl. Acad. Sci. USA 97 (2000) 14079–14084. [DOI] [PMID: 11114201]
2.	Zhan, D., Han, W. and Feng, Y. Experimental and computational studies indicate the mutation of Glu¹² to increase the thermostability of oligomeric protease from Pyrococcus horikoshii. J Mol Model 17 (2011) 1241–1249. [DOI] [PMID: 20711794]
3.	Zhan, D., Bai, A., Yu, L., Han, W. and Feng, Y. Characterization of the PH1704 protease from Pyrococcus horikoshii OT3 and the critical functions of Tyr¹²⁰. PLoS One 9:e103902 (2014). [DOI] [PMID: 25192005]

[EC 3.4.11.27 created 2023]