ID   CARP_RHIAZ              Reviewed;           7 AA.
AC   C0HLM4;
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=Rhizopuspepsin {ECO:0000305};
DE            EC=3.4.23.21 {ECO:0000269|PubMed:31219401};
DE   Flags: Fragment;
OS   Rhizopus azygosporus (Rhizopus microsporus var. azygosporus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=86630 {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 with broad specificity similar to that
CC         of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots
CC         milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but
CC         does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of
CC         insulin.; EC=3.4.23.21; Evidence={ECO:0000269|PubMed:31219401};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7 with hemoglobin as substrate.
CC         {ECO:0000269|PubMed:31219401};
CC       Temperature dependence:
CC         Optimum temperature is between 45-50 degrees Celsius with hemoglobin
CC         as substrate. Loses 50% of its activity at 60 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..>7
FT                   /note="Rhizopuspepsin"
FT                   /id="PRO_0000451149"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:31219401"
FT   NON_TER         7
FT                   /evidence="ECO:0000303|PubMed:31219401"
SQ   SEQUENCE   7 AA;  600 MW;  7772D1A862C87DB0 CRC64;
     AGVGTVP