Nuclease S1

Nuclease S1
Identifiers
EC no.3.1.30.1
CAS no.37288-25-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
S1-P1 nuclease
P1 nuclease in complex with a substrate analog
Identifiers
SymbolS1-P1_nuclease
PfamPF02265
Pfam clanCL0368
InterProIPR003154
SCOP21ak0 / SCOPe / SUPFAM
CDDcd11010
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Nuclease S1 (EC 3.1.30.1) is an endonuclease enzyme that splits single-stranded DNA (ssDNA) and RNA into oligo- or mononucleotides. This enzyme catalyses the following chemical reaction

Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products

Although its primary substrate is single-stranded, it can also occasionally introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. The enzyme hydrolyses single stranded region in duplex DNA such as loops or gaps. It also cleaves a strand opposite a nick on the complementary strand. It has no sequence specificity.

Well-known versions include S1 found in Aspergillus oryzae (yellow koji mold) and Nuclease P1 found in Penicillium citrinum. Members of the S1/P1 family are found in both prokaryotes and eukaryotes and are thought to be associated in programmed cell death and also in tissue differentiation. Furthermore, they are secreted extracellular, that is, outside of the cell. Their function and distinguishing features mean they have potential in being exploited in the field of biotechnology.