3.4.11.B7: arginyl aminopeptidase PH1704
This is an abbreviated version!
For detailed information about arginyl aminopeptidase PH1704, go to the full flat file.
Reaction
the enzyme is an aminopeptidase with limited specificity, mainly releasing the N-terminal L-arginine and hardly cleaving other amino acids. L-Arg-7-amido-4-methylcoumarin is the best artificial substrate =
Synonyms
arginine-specific aminopeptidase, PH1704, PH1704 protease
ECTree
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Reference on EC 3.4.11.B7 - arginyl aminopeptidase PH1704
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhan, D.; Han, W.; 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
1241-1249
2011
Pyrococcus horikoshii (O59413), Pyrococcus horikoshii DSM 12428 (O59413)
Zhan, D.; Bai, A.; Yu, L.; Han, W.; Feng, Y.
Characterization of the PH1704 protease from Pyrococcus horikoshii OT3 and the critical functions of Tyr120
PLoS One
9
e103902
2014
Pyrococcus horikoshii (O59413), Pyrococcus horikoshii DSM 12428 (O59413)
Du, X.; Choi, I.G.; Kim, R.; Wang, W.; Jancarik, J.; Yokota, H.; Kim, S.H.
Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2 A resolution
Proc. Natl. Acad. Sci. USA
97
14079-14084
2000
Pyrococcus horikoshii (O59413), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O59413)
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