Calf-intestinal alkaline phosphatase

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Calf-intestinal alkaline phosphatase
Identifiers
Organism Bos taurus
SymbolALPI
UniProt P19111
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Structures Swiss-model
Domains InterPro
Calf-intestinal alkaline phosphatase
Identifiers
EC no. 3.1.3.1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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NCBI proteins

Calf-intestinal alkaline phosphatase (CIAP/CIP) is a type of alkaline phosphatase that catalyzes the removal of phosphate groups from the 5' end of DNA strands and phosphomonoesters from RNA. [1] [2] This enzyme is frequently used in DNA sub-cloning, as DNA fragments that lack the 5' phosphate groups cannot ligate. [3] This prevents recircularization of the linearized DNA vector and improves the yield of the vector containing the appropriate insert.

Applications

Calf-intestinal alkaline phosphatase can serve as an effective tool for removing uranium from groundwater and soil that can pose major health risks. [4] Furthermore, the toxicity of lipopolysaccharide (LPS) was mitigated by calf-intestinal alkaline phosphatase in mice and piglets, which indicates that it could be a promising new therapeutic agent for treating diseases associated with LPS. [5]

Related Research Articles

<span class="mw-page-title-main">Lipopolysaccharide</span> Class of molecules found in the outer membrane of gram-negative bacteria

Lipopolysaccharide, now more commonly known as endotoxin, is a collective term for components of the outermost membrane of cell envelope of gram-negative bacteria, such as E. coli and Salmonella with a common structural architecture. Lipopolysaccharides (LPS) are large molecules consisting of three parts: an outer core polysaccharide termed the O-antigen, an inner core oligosaccharide and Lipid A, all covalently linked. In current terminology, the term endotoxin is often used synonymously with LPS, although there are a few endotoxins that are not related to LPS, such as the so-called delta endotoxin proteins produced by Bacillus thuringiensis.

<span class="mw-page-title-main">Alkaline phosphatase</span> Homodimeric protein enzyme

The enzyme alkaline phosphatase is a phosphatase with the physiological role of dephosphorylating compounds. The enzyme is found across a multitude of organisms, prokaryotes and eukaryotes alike, with the same general function, but in different structural forms suitable to the environment they function in. Alkaline phosphatase is found in the periplasmic space of E. coli bacteria. This enzyme is heat stable and has its maximum activity at high pH. In humans, it is found in many forms depending on its origin within the body – it plays an integral role in metabolism within the liver and development within the skeleton. Due to its widespread prevalence in these areas, its concentration in the bloodstream is used by diagnosticians as a biomarker in helping determine diagnoses such as hepatitis or osteomalacia.

<i>Sphingomonas</i> Genus of bacteria

Sphingomonas was defined in 1990 as a group of Gram-negative, rod-shaped, chemoheterotrophic, strictly aerobic bacteria. They possess ubiquinone 10 as their major respiratory quinone, contain glycosphingolipids (GSLs), specifically ceramide, instead of lipopolysaccharide (LPS) in their cell envelopes, and typically produce yellow-pigmented colonies. The GSL serves to protect the bacteria from antibacterial substances. Unlike most Gram-negative bacteria, Sphingomonas cannot carry endotoxins due to the lack of lipopolysaccharides, and has a hydrophobic surface characterized by the short nature of the GSL's carbohydrate portion.

In biochemistry, dephosphorylation is the removal of a phosphate group from an organic compound by hydrolysis. It is a reversible post-translational modification. Dephosphorylation and its counterpart, phosphorylation, activate and deactivate enzymes by detaching or attaching phosphoric esters and anhydrides. A notable occurrence of dephosphorylation is the conversion of ATP to ADP and inorganic phosphate.

<span class="mw-page-title-main">Phytase</span> Class of enzymes

A phytase is any type of phosphatase enzyme that catalyzes the hydrolysis of phytic acid – an indigestible, organic form of phosphorus that is found in many plant tissues, especially in grains and oil seeds – and releases a usable form of inorganic phosphorus. While phytases have been found to occur in animals, plants, fungi and bacteria, phytases have been most commonly detected and characterized from fungi.

<span class="mw-page-title-main">Lipopolysaccharide binding protein</span> Protein in humans

Lipopolysaccharide binding protein (LBP) is a protein that in humans is encoded by the LBP gene.

<span class="mw-page-title-main">Lymphocyte antigen 96</span> Protein-coding gene in the species Homo sapiens

Lymphocyte antigen 96, also known as "Myeloid Differentiation factor 2 (MD-2)," is a protein that in humans is encoded by the LY96 gene.

<span class="mw-page-title-main">Pancreatic ribonuclease family</span> Class of enzymes

Pancreatic ribonuclease family is a superfamily of pyrimidine-specific endonucleases found in high quantity in the pancreas of certain mammals and of some reptiles.

<span class="mw-page-title-main">ALPL</span> Protein-coding gene in the species Homo sapiens

Alkaline phosphatase, tissue-nonspecific isozyme is an enzyme that in humans is encoded by the ALPL gene.

<span class="mw-page-title-main">VIPR2</span> Protein-coding gene in the species Homo sapiens

Vasoactive intestinal peptide receptor 2 also known as VPAC2, is a G-protein coupled receptor that in humans is encoded by the VIPR2 gene.

<span class="mw-page-title-main">Bruce Beutler</span> American immunologist and geneticist

Bruce Alan Beutler is an American immunologist and geneticist. Together with Jules A. Hoffmann, he received one-half of the 2011 Nobel Prize in Physiology or Medicine, for "discoveries concerning the activation of innate immunity." Beutler discovered the long-elusive receptor for lipopolysaccharide. He did so by identifying spontaneous mutations in the gene coding for mouse Toll-like receptor 4 (Tlr4) in two unrelated strains of LPS-refractory mice and proving they were responsible for that phenotype. Subsequently, and chiefly through the work of Shizuo Akira, other TLRs were shown to detect signature molecules of most infectious microbes, in each case triggering an innate immune response.

<span class="mw-page-title-main">Inositol-phosphate phosphatase</span> Class of enzymes

The enzyme Inositol phosphate-phosphatase is of the phosphodiesterase family of enzymes. It is involved in the phosphophatidylinositol signaling pathway, which affects a wide array of cell functions, including but not limited to, cell growth, apoptosis, secretion, and information processing. Inhibition of inositol monophosphatase may be key in the action of lithium in treating bipolar disorder, specifically manic depression.

<span class="mw-page-title-main">Pancreatic polypeptide receptor 1</span> Protein-coding gene in the species Homo sapiens

Pancreatic polypeptide receptor 1, also known as Neuropeptide Y receptor type 4, is a protein that in humans is encoded by the PPYR1 gene.

<span class="mw-page-title-main">LITAF</span> Protein-coding gene in the species Homo sapiens

Lipopolysaccharide-induced tumor necrosis factor-alpha factor is a protein that in humans is encoded by the LITAF gene.

<span class="mw-page-title-main">PPAP2A</span> Protein-coding gene in the species Homo sapiens

Lipid phosphate phosphohydrolase 1 also known as phosphatidic acid phosphatase 2a is an enzyme that in humans is encoded by the PPAP2A gene.

<span class="mw-page-title-main">Homeobox protein CDX-1</span> Protein-coding gene in the species Homo sapiens

Homeobox protein CDX-1 is a protein in humans that is encoded by the CDX1 gene. CDX-1 is expressed in the developing endoderm and its expression persists in the intestine throughout adulthood. CDX-1 protein expression varies along the intestine, with high expression in intestinal crypts and diminishing expression along intestinal villi.

<span class="mw-page-title-main">ENPP7</span> Protein-coding gene in the species Homo sapiens

Ectonucleotide pyrophosphatase/phosphodiesterase family member 7 also known as alkaline sphingomyelin phosphodiesterase (Alk-SMase) or intestinal alkaline sphingomyelinase is an enzyme that in humans is encoded by the ENPP7 gene.

<span class="mw-page-title-main">Alkaline phosphatase, placental type</span> Protein-coding gene in the species Homo sapiens

Alkaline phosphatase, placental type also known as placental alkaline phosphatase (PLAP) is an allosteric enzyme that in humans is encoded by the ALPP gene.

<span class="mw-page-title-main">ALPI</span> Protein-coding gene in the species Homo sapiens

Alkaline phosphatase, intestinal also known as ALPI is a type of alkaline phosphatase that in humans is encoded by the ALPI gene.

<span class="mw-page-title-main">Ligation (molecular biology)</span> Technique for joining nucleic acid fragments

Ligation is the joining of two nucleotides, or two nucleic acid fragments, into a single polymeric chain through the action of an enzyme known as a ligase. The reaction involves the formation of a phosphodiester bond between the 3'-hydroxyl terminus of one nucleotide and the 5'-phosphoryl terminus of another nucleotide, which results in the two nucleotides being linked consecutively on a single strand. Ligation works in fundamentally the same way for both DNA and RNA. A cofactor is generally involved in the reaction, usually ATP or NAD+. Eukaryotic ligases belong to the ATP type, while the NAD+ type are found in bacteria (e.g. E. coli).

References

  1. Sambrook J, Fritsch EF, Maniatis T (1989). Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory.
  2. Seeburg PH, Shine J, Martial JA, Baxter JD, Goodman HM (December 1977). "Nucleotide sequence and amplification in bacteria of structural gene for rat growth hormone". Nature. 270 (5637): 486–494. Bibcode:1977Natur.270..486S. doi:10.1038/270486a0. PMID   339105. S2CID   4196683.
  3. Ullrich A, Shine J, Chirgwin J, Pictet R, Tischer E, Rutter WJ, Goodman HM (June 1977). "Rat insulin genes: construction of plasmids containing the coding sequences". Science. 196 (4296). New York, N.Y.: 1313–1319. Bibcode:1977Sci...196.1313U. doi:10.1126/science.325648. PMID   325648.
  4. Chaudhuri G, Dey P, Dalal D, Venu-Babu P, Thilagaraj WR (July 2013). "A Novel Approach to Precipitation of Heavy Metals from Industrial Effluents and Single-Ion Solutions Using Bacterial Alkaline Phosphatase". Water, Air, & Soil Pollution. 224 (7): 1625. Bibcode:2013WASP..224.1625C. doi:10.1007/s11270-013-1625-y. ISSN   0049-6979. S2CID   97367168.
  5. Beumer C, Wulferink M, Raaben W, Fiechter D, Brands R, Seinen W (November 2003). "Calf intestinal alkaline phosphatase, a novel therapeutic drug for lipopolysaccharide (LPS)-mediated diseases, attenuates LPS toxicity in mice and piglets". The Journal of Pharmacology and Experimental Therapeutics. 307 (2): 737–744. doi:10.1124/jpet.103.056606. PMID   12970380. S2CID   15049304.