Serratia marcescens nuclease

Serratia marcescens nuclease
Serratia marcescens nuclease
Identifiers
Organism	Serratia marcescens
Symbol	nucA
UniProt	P13717
Structures
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Structures	Swiss-model
Domains	InterPro

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Serratia marcescens nuclease
Serratia marcescens nuclease
Identifiers
EC no.	3.1.30.2
CAS no.	9025-65-4
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Serratia marcescens nuclease (EC 3.1.30.2, endonuclease (Serratia marcescens), barley nuclease, plant nuclease I, nucleate endonuclease) is an enzyme.^[1]^[2]^[3]^[4] This enzyme catalyses the following chemical reaction

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

Hydrolyses double- or single-stranded substrate. It is a representative of the DNA/RNA non-specific endonuclease family.

References[]

^ Mikulski AJ, Laskowski M (October 1970). "Mung bean nuclease I. 3. Purification procedure and (3') omega monophosphatase activity". The Journal of Biological Chemistry. 245 (19): 5026–31. PMID 4319109.
^ Stevens, A.; Hilmoe, R.J. (1960). "Studies on a nuclease from Azotobacter agilis. I. Isolation and mode of action". J. Biol. Chem. 235: 3016–3022.
^ Stevens A, Hilmoe RJ (1960). "Studies on a nuclease from Azotobacter agilis. II. Hydrolysis of ribonucleic and deoxyribonucleic acids". J. Biol. Chem. 235: 3023–3027.
^ Wechter WJ, Mikulski AJ, Laskowski M (February 1968). "Gradation of specificity with regard to sugar among nucleases". Biochemical and Biophysical Research Communications. 30 (3): 318–22. doi:10.1016/0006-291x(68)90453-1. PMID 4296679.

External links[]

Serratia+marcescens+nuclease at the US National Library of Medicine Medical Subject Headings (MeSH)
Serratia marcescens endonuclease at Protean Ltd., highly active

[1] Mikulski AJ, Laskowski M (October 1970). "Mung bean nuclease I. 3. Purification procedure and (3') omega monophosphatase activity". The Journal of Biological Chemistry. 245 (19): 5026–31. PMID 4319109.

[2] Stevens, A.; Hilmoe, R.J. (1960). "Studies on a nuclease from Azotobacter agilis. I. Isolation and mode of action". J. Biol. Chem. 235: 3016–3022.

[3] Stevens A, Hilmoe RJ (1960). "Studies on a nuclease from Azotobacter agilis. II. Hydrolysis of ribonucleic and deoxyribonucleic acids". J. Biol. Chem. 235: 3023–3027.

[4] Wechter WJ, Mikulski AJ, Laskowski M (February 1968). "Gradation of specificity with regard to sugar among nucleases". Biochemical and Biophysical Research Communications. 30 (3): 318–22. doi:10.1016/0006-291x(68)90453-1. PMID 4296679.

[1]

[2]

[3]

[4]

v t Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)