PHE_STRMO
ID PHE_STRMO Reviewed; 14 AA.
AC P81801;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Puromycin-hydrolyzing enzyme;
DE EC=3.-.-.-;
DE Flags: Fragment;
OS Streptomyces morookaense (Streptoverticillium morookaense).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1970;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=ATCC 19166 / DSM 40503 / JCM 4673 / KCC S-0673 / NBRC 13416 / NRRL
RC B-12429 / VKM Ac-1916;
RX PubMed=9538199; DOI=10.1093/oxfordjournals.jbchem.a021929;
RA Nishimura M., Matsuo H., Nakamura A., Sugiyama M.;
RT "Purification and characterization of a puromycin-hydrolyzing enzyme from
RT blasticidin S-producing Streptomyces morookaensis.";
RL J. Biochem. 123:247-252(1998).
RN [2]
RP CHARACTERIZATION, AND FUNCTION.
RA Nishimura M., Matsuo H., Sugiyama M.;
RT "Blasticidin S-producing Streptomyces morookaensis possesses an enzyme
RT activity with hydrolyzes puromycin.";
RL FEMS Microbiol. Lett. 132:95-100(1995).
CC -!- FUNCTION: Inactivates puromycin by catalyzing the hydrolysis of the
CC amide linkage between its aminonucleoside and O-methyl-L-tyrosine
CC moieties. May have aminopeptidase activity. {ECO:0000269|Ref.2}.
CC -!- ACTIVITY REGULATION: Stimulated by DTT. Strongly inhibited by zinc ion,
CC Fe(2+) ion, Cu(2+) ion, mercury ion, N-bromosuccinimide and N-
CC ethylmaleimide. Partially inhibited by cobalt ion.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0.;
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.;
CC -!- SUBUNIT: Monomer.
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DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Aminopeptidase; Direct protein sequencing; Hydrolase; Protease.
FT CHAIN 1..>14
FT /note="Puromycin-hydrolyzing enzyme"
FT /id="PRO_0000058378"
FT NON_TER 14
SQ SEQUENCE 14 AA; 1492 MW; 3F980730E45EF3D8 CRC64;
VSTAPYGAWQ SPID