Micrococcal nuclease | |||||||||
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![]() Ribbon schematic of micrococcal nuclease 3D structure, with Ca2+ and TdtP inhibitor | |||||||||
Identifiers | |||||||||
EC no. | 3.1.31.1 | ||||||||
CAS no. | 9013-53-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Thermonuclease | |||||||
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Identifiers | |||||||
Organism | |||||||
Symbol | nuc | ||||||
UniProt | P00644 | ||||||
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Staphylococcal nuclease | |||||||||
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Identifiers | |||||||||
Symbol | ? | ||||||||
Pfam | PF00565 | ||||||||
Pfam clan | CL0049 | ||||||||
InterPro | IPR016071 | ||||||||
PROSITE | PDOC00865 | ||||||||
CATH | 1tt2 | ||||||||
SCOP2 | 1tt2 / SCOPe / SUPFAM | ||||||||
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Micrococcal nuclease ( EC 3.1.31.1, S7 Nuclease, MNase, spleen endonuclease, thermonuclease, nuclease T, micrococcal endonuclease, nuclease T', staphylococcal nuclease, spleen phosphodiesterase, Staphylococcus aureus nuclease, Staphylococcus aureus nuclease B, ribonucleate (deoxynucleate) 3'-nucleotidohydrolase) is an endo- exonuclease that preferentially digests single-stranded nucleic acids. The rate of cleavage is 30 times greater at the 5' side of A or T than at G or C and results in the production of mononucleotides and oligonucleotides with terminal 3'- phosphates. The enzyme is also active against double-stranded DNA and RNA and all sequences will be ultimately cleaved.
The enzyme has a molecular weight of 16.9kDa.
The pH optimum is reported as 9.2. The enzyme activity is strictly dependent on Ca2+ and the pH optimum varies according to Ca2+ concentration. [1] The enzyme is therefore easily inactivated by EGTA.
This enzyme is the extracellular nuclease of Staphylococcus aureus. Two strains, V8 and Foggi, yield almost identical enzymes. [2] A common source is E.coli cells carrying a cloned nuc gene encoding Staphylococcus aureus extracellular nuclease (micrococcal nuclease).
The 3-dimensional structure of micrococcal nuclease (then called Staphyloccal nuclease) was solved very early in the history of protein crystallography, in 1969, [3] deposited as now-obsolete Protein Data Bank file 1SNS. Higher-resolution, more recent crystal structures are available for the apo form as Protein Data Bank file 1SNO: [1] and for the thymidine-diphosphate-inhibited form as Protein Data Bank file 3H6M: [2] or 1SNC: [3]. As seen in the ribbon diagram above, the nuclease molecule has 3 long alpha helices and a 5-stranded, barrel-shaped beta sheet, in an arrangement known as the OB-fold (for oligonucleotide-binding fold) as classified in the SCOP database.
Micrococcal nuclease | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() Ribbon schematic of micrococcal nuclease 3D structure, with Ca2+ and TdtP inhibitor | |||||||||
Identifiers | |||||||||
EC no. | 3.1.31.1 | ||||||||
CAS no. | 9013-53-0 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
|
Thermonuclease | |||||||
---|---|---|---|---|---|---|---|
Identifiers | |||||||
Organism | |||||||
Symbol | nuc | ||||||
UniProt | P00644 | ||||||
|
Staphylococcal nuclease | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
Symbol | ? | ||||||||
Pfam | PF00565 | ||||||||
Pfam clan | CL0049 | ||||||||
InterPro | IPR016071 | ||||||||
PROSITE | PDOC00865 | ||||||||
CATH | 1tt2 | ||||||||
SCOP2 | 1tt2 / SCOPe / SUPFAM | ||||||||
|
Micrococcal nuclease ( EC 3.1.31.1, S7 Nuclease, MNase, spleen endonuclease, thermonuclease, nuclease T, micrococcal endonuclease, nuclease T', staphylococcal nuclease, spleen phosphodiesterase, Staphylococcus aureus nuclease, Staphylococcus aureus nuclease B, ribonucleate (deoxynucleate) 3'-nucleotidohydrolase) is an endo- exonuclease that preferentially digests single-stranded nucleic acids. The rate of cleavage is 30 times greater at the 5' side of A or T than at G or C and results in the production of mononucleotides and oligonucleotides with terminal 3'- phosphates. The enzyme is also active against double-stranded DNA and RNA and all sequences will be ultimately cleaved.
The enzyme has a molecular weight of 16.9kDa.
The pH optimum is reported as 9.2. The enzyme activity is strictly dependent on Ca2+ and the pH optimum varies according to Ca2+ concentration. [1] The enzyme is therefore easily inactivated by EGTA.
This enzyme is the extracellular nuclease of Staphylococcus aureus. Two strains, V8 and Foggi, yield almost identical enzymes. [2] A common source is E.coli cells carrying a cloned nuc gene encoding Staphylococcus aureus extracellular nuclease (micrococcal nuclease).
The 3-dimensional structure of micrococcal nuclease (then called Staphyloccal nuclease) was solved very early in the history of protein crystallography, in 1969, [3] deposited as now-obsolete Protein Data Bank file 1SNS. Higher-resolution, more recent crystal structures are available for the apo form as Protein Data Bank file 1SNO: [1] and for the thymidine-diphosphate-inhibited form as Protein Data Bank file 3H6M: [2] or 1SNC: [3]. As seen in the ribbon diagram above, the nuclease molecule has 3 long alpha helices and a 5-stranded, barrel-shaped beta sheet, in an arrangement known as the OB-fold (for oligonucleotide-binding fold) as classified in the SCOP database.