| 词条 | S1 P1 nuclease protein domain |
| 释义 |
| Symbol = S1-P1_nuclease | Name = S1-P1 nuclease | image = PDB 1ak0 EBI.jpg | width = | caption = P1 nuclease in complex with a substrate analog | Pfam = PF02265 | Pfam_clan = CL0368 | InterPro = IPR003154 | SMART = | PROSITE = | MEROPS = | SCOP = 1ak0 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} In molecular biology, S1 P1 nuclease refers to a protein domain with enzyme activity.This family contains both S1 and P1 nucleases (EC) which cleave RNA and single stranded DNA with no sequence specificity. They 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.[1] FunctionThe function of the P1/S1 nuclease, is to digest single-stranded (ss)RNA and DNA. It is a 36 kDa glycoprotein with very distinguishing features, they are:
These requirements and distinguishing features are responsible for function efficacy. It is an enzyme and these four features are needed for enzyme functionality. The three zinc ions are vital for catalysis. The first two zincs activate the attacking water in hydrolysis whilst the third zinc ion stabilizes the leaving oxyanion.[2][3] MechanismThis zinc-dependent nuclease protein domain produces 5' nucleotides and cleaves phosphate groups from 3' nucleotides. Additionally, the side chain of tryptophan located in the cavity in the active site and its backbone supports the action one of the zinc ions. Such mechanisms are essential to the catalytic function of the enzyme.[1] References1. ^1 {{cite journal|vauthors=Balabanova LA, Gafurov YM, Pivkin MV, Terentyeva NA, Likhatskaya GN, Rasskazov VA | title=An extracellular S1-type nuclease of marine fungus Penicillium melinii. | journal=Mar Biotechnol (NY) | year= 2012 | volume= 14 | issue= 1 | pages= 87–95 | pmid=21647618 | doi=10.1007/s10126-011-9392-5 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=21647618 }} {{InterPro content|IPR003154}}2. ^{{cite journal|vauthors=Podzimek T, Matoušek J, Lipovová P, Poučková P, Spiwok V, Santrůček J | title=Biochemical properties of three plant nucleases with anticancer potential. | journal=Plant Sci | year= 2011 | volume= 180 | issue= 2 | pages= 343–51 | pmid=21421379 | doi=10.1016/j.plantsci.2010.10.006 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=21421379 }} 3. ^{{cite journal|vauthors=Romier C, Dominguez R, Lahm A, Dahl O, Suck D | title=Recognition of single-stranded DNA by nuclease P1: high resolution crystal structures of complexes with substrate analogs. | journal=Proteins | year= 1998 | volume= 32 | issue= 4 | pages= 414–24 | pmid=9726413 | doi= 10.1002/(sici)1097-0134(19980901)32:4<414::aid-prot2>3.0.co;2-g| pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=9726413 }} 3 : Protein domains|Protein families|Nucleases |
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