ID   CARP_MUCTH              Reviewed;          10 AA.
AC   C0HLM5;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   02-DEC-2020, entry version 2.
DE   RecName: Full=Mucorpepsin {ECO:0000305};
DE            EC=3.4.23.23 {ECO:0000269|PubMed:31219401};
DE   Flags: Fragment;
OS   Mucor thermohyalospora (Soil fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=2653441 {ECO:0000303|PubMed:31219401};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   BIOTECHNOLOGY.
RX   PubMed=31219401; DOI=10.1080/10826068.2019.1630647;
RA   Chinmayee C.V., Vidya C., Rani A., Singh S.A.;
RT   "Production of highly active fungal milk-clotting enzyme by solid-state
RT   fermentation.";
RL   Prep. Biochem. Biotechnol. 49:858-867(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins, favoring hydrophobic residues at P1
CC         and P1'. Clots milk. Does not accept Lys at P1, and hence does not
CC         activate trypsinogen.; EC=3.4.23.23;
CC         Evidence={ECO:0000269|PubMed:31219401};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6 with hemoglobin as substrate. Activity decreases from
CC         pH 7, with a 36% decrease in activity when incubated at pH 10.
CC         {ECO:0000269|PubMed:31219401};
CC       Temperature dependence:
CC         Optimum temperature is between 45-55 degrees Celsius with hemoglobin
CC         as substrate. Loses 50% of its activity at 65 degrees Celsius.
CC         {ECO:0000269|PubMed:31219401};
CC   -!- BIOTECHNOLOGY: This enzyme is capable of clotting milk and thus can be
CC       used for cheese production. {ECO:0000269|PubMed:31219401}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Direct protein sequencing; Hydrolase; Protease.
FT   CHAIN           <1..>10
FT                   /note="Mucorpepsin"
FT                   /id="PRO_0000451150"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:31219401"
FT   NON_TER         10
FT                   /evidence="ECO:0000303|PubMed:31219401"
SQ   SEQUENCE   10 AA;  947 MW;  3930AFB2D5B87AA8 CRC64;
     AEGDGSVDTP