MDO2_ANAMC
ID MDO2_ANAMC Reviewed; 27 AA.
AC P83447;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Macrodontain-2;
DE EC=3.4.22.-;
DE AltName: Full=Macrodontain II;
DE Flags: Fragment;
OS Ananas macrodontes (False pineapple) (Pseudananas macrodontes).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=203992;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Fruit;
RX PubMed=11517945; DOI=10.1515/bc.2001.108;
RA Lopez L.M.I., Sequeiros C., Trejo S.A., Pardo M.F., Caffini N.O.,
RA Natalucci C.L.;
RT "Comparison of two cysteine endopeptidases from Pseudananas macrodontes
RT (Morr.) Harms (Bromeliaceae).";
RL Biol. Chem. 382:875-878(2001).
CC -!- FUNCTION: Cysteine protease that shows preferential cleavage as
CC follows: Ala-|-Xaa > Gln-|-Xaa > Tyr-Xaa. Hydrolyzes the synthetic
CC peptide substrate Bz-Phe-Val-Arg-pNA. {ECO:0000269|PubMed:11517945}.
CC -!- ACTIVITY REGULATION: Inhibited by the general cysteine protease
CC inhibitor E-64 (L-trans-epoxysuccinyl-leucylamide-(4-guanido)-butane).
CC {ECO:0000269|PubMed:11517945}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.9 uM for Bz-Phe-Val-Arg-pNA {ECO:0000269|PubMed:11517945};
CC pH dependence:
CC Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:11517945};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11517945}.
CC -!- MASS SPECTROMETRY: Mass=23703; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11517945};
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR AlphaFoldDB; P83447; -.
DR MEROPS; C01.161; -.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Protease; Thiol protease.
FT CHAIN 1..>27
FT /note="Macrodontain-2"
FT /id="PRO_0000050562"
FT NON_TER 27
SQ SEQUENCE 27 AA; 3037 MW; 118D1932988BCF98 CRC64;
AVPQSIDWRD YGAVNEVKNQ NPCGSCW