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Literature summary for 3.1.30.1 extracted from

  • Balabanova, L.; Gafurov, Y.; Pivkin, M.; Terentyeva, N.; Likhatskaya, G.; Rasskazov, V.
    An extracellular S1-type nuclease of marine fungus Penicillium melinii (2012), Mar. Biotechnol., 14, 87-95.
    View publication on PubMed
Search for more literature for 3.1.30.1

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol
-
 Penicillium melinii
EDTA reversible by Zn2+ Penicillium melinii
iodoacetamide
-
 Penicillium melinii
KH2PO4
-
 Penicillium melinii
additional information urea does not influence the enzyme at any concentrations Penicillium melinii
potassium citrate complete inhibition at 10 mM Penicillium melinii
SDS
-
 Penicillium melinii

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Penicillium melinii
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ can only partially substitute for Zn2+ Penicillium melinii
Co2+ can only partially substitute for Zn2+ Penicillium melinii
Fe2+ can only partially substitute for Zn2+ Penicillium melinii
KCl required Penicillium melinii
Mn2+ can only partially substitute for Zn2+ Penicillium melinii
NaCl required Penicillium melinii
Zn2+ required Penicillium melinii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
 gel filtration Penicillium melinii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Penicillium melinii the enzyme is active on DNA and RNA, the enzyme endonucleolytically degrades ssDNA and RNA by 3'-5' mode to produce 5'-oligonucleotides and 5'-mononucleotides. It preferentially degrades poly(U), substrate specificity, overview ?
-
 ?
poly(U) + H2O Penicillium melinii preferred substrate ?
-
 ?

Organism

Organism UniProt Comment Textmining
Penicillium melinii
-
 isolated from colonial ascidium collected near Shikotan Island, Sea of Okhotsk, at a depth of 123 m
-

Purification (Commentary)

Purification (Comment) Organism
extracellular enzyme 165fold by chromatography with modified chitosan Penicillium melinii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
41250
-
 purified enzyme, pH 3.7, 75°C Penicillium melinii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is active on DNA and RNA, the enzyme endonucleolytically degrades ssDNA and RNA by 3'-5' mode to produce 5'-oligonucleotides and 5'-mononucleotides. It preferentially degrades poly(U), substrate specificity, overview Penicillium melinii ?
-
 ?
poly(U) + H2O preferred substrate Penicillium melinii ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 35000, SDS-PAGE Penicillium melinii

Synonyms

Synonyms Comment Organism
S1-type nuclease
-
 Penicillium melinii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
75
-
-
 Penicillium melinii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.7
-
-
 Penicillium melinii

pH Range

pH Minimum pH Maximum Comment Organism
2.5 8 activity range Penicillium melinii

General Information

General Information Comment Organism
additional information mode of nuclease action and molecular modeling, overview Penicillium melinii
physiological function tight correlation found between the extracellular endonuclease activity and the rate of thymidine uptake by actively growing cells suggesting that this nuclease is required for fulfilling the nucleotide pool of precursors of DNA biosynthesis during the transformation of hyphae into the aerial mycelium and conidia in stressful environmental conditions Penicillium melinii