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Phosphate Transporter
Phosphate permeases are membrane transport proteins that facilitate the diffusion of phosphate into and out of a cell or organelle. Some of these families include: TC# 2.A.1.4Organophosphate:Pi Antiporter (OPA) Family (i.e., Pho-84 of ''Neurospora crassa''TC# 2.A.1.9.2 TC# 2.A.20- Inorganic Phosphate Transporter (PiT) Family TC# 2.A.47.2- Phosphate porters of the Divalent Anion:Na+ Symporter (DASS) Family, includes Pho87/90/91 TC# 2.A.58- Phosphate:Na+ Symporter (PNaS) Family TC# 2.A.94- Phosphate Permease (Pho1) Family See also * Major facilitator superfamily * Ion transporter superfamily * Phosphotransferase * Inorganic phosphate * permeases * Transporter Classification Database See also TC# 3.A.10- H+, Na+-translocating Pyrophosphatase (M+-PPase) Family TC# 4.E.1- Vacuolar (Acidocalcisome) Polyphosphate Polymerase (V-PPP) Family Further reading * EMBL-EBI, InterPro [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Inorganic Phosphate Transporter Family
The inorganic phosphate transporter (PiT) family is a group of carrier proteins derived from Gram-negative bacteria, Gram-negative and Gram-positive bacteria, archaea, and eukaryotes. Function Functionally-characterized members of the family appear to catalyze Inorganic phosphate, inorganic phosphate (Pi) or inorganic sulfate uptake either by H+ or Na+ Symporter, symport. Both PitATC# 2.A.20.1.1 and PitBTC# 2.A.20.1.2 of ''E. coli'' probably catalyze metal ion·phosphate:H+ symport, where Mg2+, Ca2+ or Zn2+ (and probably other divalent cations) can complex with Pi. The mammalian proteins (i.e.TC# 2.A.20.2.7 have been reported to function as viral receptors, but they undoubtedly function as transport proteins as well. For numerous Retrovirus, gammaretroviruses, such as the gibbon ape leukemia virus, woolly monkey virus, feline leukemia virus subgroup B, feline leukemia virus subgroup T, and 10A1 murine leukemia virus, this receptor is the human type III sodium-dependent inorganic p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PubMed Central
PubMed Central (PMC) is a free digital repository that archives open access full-text scholarly articles that have been published in biomedical and life sciences journals. As one of the major research databases developed by the National Center for Biotechnology Information (NCBI), PubMed Central is more than a document repository. Submissions to PMC are indexed and formatted for enhanced metadata, medical ontology, and unique identifiers which enrich the XML structured data for each article. Content within PMC can be linked to other NCBI databases and accessed via Entrez search and retrieval systems, further enhancing the public's ability to discover, read and build upon its biomedical knowledge. PubMed Central is distinct from PubMed. PubMed Central is a free digital archive of full articles, accessible to anyone from anywhere via a web browser (with varying provisions for reuse). Conversely, although PubMed is a searchable database of biomedical citations and abstracts, the ful ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Digital Object Identifier
A digital object identifier (DOI) is a persistent identifier or handle used to uniquely identify various objects, standardized by the International Organization for Standardization (ISO). DOIs are an implementation of the Handle System; they also fit within the URI system ( Uniform Resource Identifier). They are widely used to identify academic, professional, and government information, such as journal articles, research reports, data sets, and official publications. DOIs have also been used to identify other types of information resources, such as commercial videos. A DOI aims to resolve to its target, the information object to which the DOI refers. This is achieved by binding the DOI to metadata about the object, such as a URL where the object is located. Thus, by being actionable and interoperable, a DOI differs from ISBNs or ISRCs which are identifiers only. The DOI system uses the indecs Content Model for representing metadata. The DOI for a document remains fixed over t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PubMed Identifier
PubMed is a free search engine accessing primarily the MEDLINE database of references and abstracts on life sciences and biomedical topics. The United States National Library of Medicine (NLM) at the National Institutes of Health maintain the database as part of the Entrez system of information retrieval. From 1971 to 1997, online access to the MEDLINE database had been primarily through institutional facilities, such as university libraries. PubMed, first released in January 1996, ushered in the era of private, free, home- and office-based MEDLINE searching. The PubMed system was offered free to the public starting in June 1997. Content In addition to MEDLINE, PubMed provides access to: * older references from the print version of ''Index Medicus'', back to 1951 and earlier * references to some journals before they were indexed in Index Medicus and MEDLINE, for instance ''Science'', ''BMJ'', and ''Annals of Surgery'' * very recent entries to records for an article before it ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
International Standard Serial Number
An International Standard Serial Number (ISSN) is an eight-digit serial number used to uniquely identify a serial publication, such as a magazine. The ISSN is especially helpful in distinguishing between serials with the same title. ISSNs are used in ordering, cataloging, interlibrary loans, and other practices in connection with serial literature. The ISSN system was first drafted as an International Organization for Standardization (ISO) international standard in 1971 and published as ISO 3297 in 1975. ISO subcommittee TC 46/SC 9 is responsible for maintaining the standard. When a serial with the same content is published in more than one media type, a different ISSN is assigned to each media type. For example, many serials are published both in print and electronic media. The ISSN system refers to these types as print ISSN (p-ISSN) and electronic ISSN (e-ISSN). Consequently, as defined in ISO 3297:2007, every serial in the ISSN system is also assigned a linking ISSN ( ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Polyphosphate Kinase
In enzymology, a polyphosphate kinase (), or polyphosphate polymerase, is an enzyme that catalyzes the formation of polyphosphate from ATP, with chain lengths of up to a thousand or more orthophosphate moieties. :ATP + (phosphate)n \rightleftharpoons ADP + (phosphate)n+1 Thus, the two substrates of this enzyme are ATP and polyphosphate phosphate)n whereas its two products are ADP and polyphosphate extended by one phosphate moiety phosphate)n+1 This enzyme is a membrane protein and goes through an intermediate stage during the reaction where it is autophosphorylated with a phosphate group covalently linked to a basic amino acyl residue through an N-P bond. Several enzymes catalyze polyphosphate polymerization. Some of these enzymes couple phosphotransfer to transmembrane transport. These enzyme/transporters are categorized in the Transporter Classification Database (TCDB) under the Polyphosphate Polymerase/YidH SuperfamilyTC# 4.E.1 and are transferases that transfer ph ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
H+, Na+-translocating Pyrophosphatase Family
Members of the H+, Na+-translocating Pyrophosphatase (M+''-PPase)'' FamilyTC# 3.A.10 are found in the vacuolar (tonoplast) membranes of higher plants, algae, and protozoa, and in both bacteria and archaea. They are therefore ancient enzymes. Two types of inorganic diphosphatase, very different in terms of both amino acid sequence and structure, have been characterised to date: soluble and transmembrane proton-pumping pyrophosphatases (sPPases and H(+)-PPases, respectively). sPPases are ubiquitous proteins that hydrolyse pyrophosphate to release heat, whereas H+-PPases, so far unidentified in animal and fungal cells, couple the energy of PPi hydrolysis to proton movement across biological membranes. The latter type is represented by this group of proteins. H+-PPases vacuolar-type inorganic pyrophosphatases (V-PPase) or pyrophosphate-energised vacuolar membrane proton pumps. In plants, vacuoles contain two enzymes for acidifying the interior of the vacuole, the V-ATPase and th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Permease
The permeases are membrane transport proteins, a class of multipass transmembrane proteins that allow the diffusion of a specific molecule in or out of the cell in the direction of a concentration gradient, a form of facilitated diffusion. The permease binding is first step of translocation. LacY protein from Escherichia coli is an example of a permease. See also * Lactose permease * Beta-galactoside permease It was originally discovered in the 1930s by Joy Adames. It is a transporter protein that helps in various aspects of cellular life including DNA replication, translation of RNA, and diffusion. * Amino acid permease Amino acid permeases are membrane permeases involved in the transport of amino acids into the cell. A number of such proteins have been found to be evolutionary related. These proteins contain 12 transmembrane segments. See also *Amino acid tra ... A permease (porter) is a protein or protein complex that catalyzes a vectorial reaction, irrespective of whether ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphate
In chemistry, a phosphate is an anion, salt, functional group or ester derived from a phosphoric acid. It most commonly means orthophosphate, a derivative of orthophosphoric acid . The phosphate or orthophosphate ion is derived from phosphoric acid by the removal of three protons . Removal of one or two protons gives the dihydrogen phosphate ion and the hydrogen phosphate ion ion, respectively. These names are also used for salts of those anions, such as ammonium dihydrogen phosphate and trisodium phosphate. File:3-phosphoric-acid-3D-balls.png, Phosphoricacid File:2-dihydrogenphosphate-3D-balls.png, Dihydrogenphosphate File:1-hydrogenphosphate-3D-balls.png, Hydrogenphosphate File:0-phosphate-3D-balls.png, Phosphate In organic chemistry, phosphate or orthophosphate is an organophosphate, an ester of orthophosphoric acid of the form where one or more hydrogen atoms are replaced by organic groups. An example is trimethyl phosphate, . The term also refers to the triv ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phosphotransferase
Phosphotransferases are a category of enzymes ( EC number 2.7) that catalyze phosphorylation reactions. The general form of the reactions they catalyze is: :A-P + B \rightleftharpoons B-P + A Where ''P'' is a phosphate group and A and B are the donating and accepting molecules, respectively. Classification Phosphotransferases are generally classified according to the acceptor molecule. , Classification in this article follows the rules of Enzyme Nomenclature of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). *EC 2.7.1 Phosphotransferases with an as acceptor *EC 2.7.2 Phosphotransferases with a |
