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Plant-specific Insert
The plant-specific insert (PSI) or plant-specific sequence (PSS) is an independent domain, exclusively found in plants, consisting of approximately 100 residues, found on the C-terminal lobe on some aspartic proteases (AP) called phytepsins. The PSI, as an independent entity separate from its parent AP, is homologous to saposin and belongs to the saposin-like protein family (SAPLIP). Although the PSI is grouped along proteins in the SAPLIP family, the PSI does not contain a proper saposin-like domain. This is due to a circular permutation of the N- and C-termini of the PSI, in which the termini are "swapped". This has led to the PSI being termed a "swaposin" (a play-on-words of "swap" and "saposin") although the tertiary structure still remains homologous to saposin and other members of the SAPLIP family. Structure Among plants, APs between different species are generally homologous exhibiting high sequence identity whilst maintaining a similar tertiary structure to pepsin. As ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aspartate Protease
Aspartic proteases are a catalytic type of protease enzymes that use an activated water molecule bound to one or more aspartate residues for catalysis of their peptide substrates. In general, they have two highly conserved aspartates in the active site and are optimally active at acidic pH. Nearly all known aspartyl proteases are inhibited by pepstatin. Aspartic endopeptidases of vertebrate, fungal and retroviral origin have been characterised. More recently, aspartic endopeptidases associated with the processing of bacterial type 4 prepilin and archaean preflagellin have been described. Eukaryotic aspartic proteases include pepsins, cathepsins, and renins. They have a two-domain structure, arising from ancestral duplication. Retroviral and retrotransposon proteases (retroviral aspartyl proteases) are much smaller and appear to be homologous to a single domain of the eukaryotic aspartyl proteases. Each domain contributes a catalytic Asp residue, with an extended active site c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Granulysin
Granulysin (GNLY) is a protein expressed in most mammals which functions as an antimicrobial peptide released by killer lymphocytes in cytotoxic granules. It is a pore-forming peptide, as it can puncture a microbial cell wall, allowing for other death-inducing enzymes to enter the microbe and cause microptosis. GNLY is inhibited by cholesterol, and is most effective in helping to kill cholesterol-deficient microbes. It is part of the saponin-like protein family, and its gene is found on the 2nd chromosome in humans. It is distinguished by its 5 α-helical structure. Its expression is restricted to cytotoxic immune cells such as cytotoxic T cells, NK cells, NKT cells and γδ T cells. Orthologs of this protein are found in most mammal species, such as in cows and pigs, however not in rodents. Granulysin is also an active player in many diseases, including Leprosy and Toxic Epidermal Necrolysis. Structure Granulysin has a five alpha-helix structure, and is part of the saposin-lik ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Prosaposin
Prosaposin, also known as PSAP, is a protein which in humans is encoded by the ''PSAP'' gene. This highly conserved glycoprotein is a precursor for 4 cleavage products: saposins A, B, C, and D. Saposin is an acronym for Sphingolipid Activator PrO ''SeINs. Each domain of the precursor protein is approximately 80 amino acid residues long with nearly identical placement of cysteine residues and glycosylation sites. Saposins A-D localize primarily to the lysosomal compartment where they facilitate the catabolism of glycosphingolipids with short oligosaccharide groups. The precursor protein exists both as a secretory protein and as an integral membrane protein and has neurotrophic activities. Saposins A–D are required for the hydrolysis of certain sphingolipids by specific lysosomal hydrolases. Family members * Saposin A was identified as an N-terminal domain in the prosaposin cDNA prior to its isolation. It is known to stimulate the enzymatic hydrolysis of 4-methylumbelliferyl-β ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Michaelis–Menten Kinetics
In biochemistry, Michaelis–Menten kinetics is one of the best-known models of enzyme kinetics. It is named after German biochemist Leonor Michaelis and Canadian physician Maud Menten. The model takes the form of an equation describing the rate of enzymatic reactions, by relating reaction rate v (rate of formation of product, ce P/math>) to ce S/math>, the concentration of a substrate ''S''. Its formula is given by : v = \frac = V_\max \frac This equation is called the Michaelis–Menten equation. Here, V_\max represents the maximum rate achieved by the system, happening at saturating substrate concentration for a given enzyme concentration. When the value of the Michaelis constant K_\mathrm is numerically equal to the substrate concentration, then the reaction rate is half of V_\max. Biochemical reactions involving a single substrate are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions. Model In 1901, French ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Potato
The potato is a starchy food, a tuber of the plant ''Solanum tuberosum'' and is a root vegetable native to the Americas. The plant is a perennial in the nightshade family Solanaceae. Wild potato species can be found from the southern United States to southern Chile. The potato was originally believed to have been domesticated by Native Americans independently in multiple locations,University of Wisconsin-Madison, ''Finding rewrites the evolutionary history of the origin of potatoes'' (2005/ref> but later genetic studies traced a single origin, in the area of present-day southern Peru and extreme northwestern Bolivia. Potatoes were domesticated there approximately 7,000–10,000 years ago, from a species in the ''Solanum brevicaule'' complex. Lay summary: In the Andes region of South America, where the species is indigenous, some close relatives of the potato are cultivated. Potatoes were introduced to Europe from the Americas by the Spanish in the second half of the 16 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Atomic Force Microscopy
Atomic force microscopy (AFM) or scanning force microscopy (SFM) is a very-high-resolution type of scanning probe microscopy (SPM), with demonstrated resolution on the order of fractions of a nanometer, more than 1000 times better than the optical diffraction limit. Overview Atomic force microscopy (AFM) is a type of scanning probe microscopy (SPM), with demonstrated resolution on the order of fractions of a nanometer, more than 1000 times better than the optical diffraction limit. The information is gathered by "feeling" or "touching" the surface with a mechanical probe. Piezoelectric elements that facilitate tiny but accurate and precise movements on (electronic) command enable precise scanning. Despite the name, the Atomic Force Microscope does not use the Nuclear force. Abilities The AFM has three major abilities: force measurement, topographic imaging, and manipulation. In force measurement, AFMs can be used to measure the forces between the probe and the sample as ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Botrytis Cinerea
''Botrytis cinerea'' is a necrotrophic fungus that affects many plant species, although its most notable hosts may be wine grapes. In viticulture, it is commonly known as "botrytis bunch rot"; in horticulture, it is usually called "grey mould" or "gray mold". The fungus gives rise to two different kinds of infections on grapes. The first, grey rot, is the result of consistently wet or humid conditions, and typically results in the loss of the affected bunches. The second, noble rot, occurs when drier conditions follow wetter, and can result in distinctive sweet dessert wines, such as Sauternes (wine), Sauternes or the Aszú of Tokaji/Grasă de Cotnari. The species name ''Botrytis cinerea'' is derived from the Latin for "grapes like ashes"; although poetic, the "grapes" refers to the bunching of the fungal spores on their Conidium, conidiophores, and "ashes" just refers to the greyish colour of the spores ''en masse''. The fungus is usually referred to by its anamorph (asexual form ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AOAH
Acyloxyacyl hydrolase, also known as AOAH, is a protein which in humans is encoded by the ''AOAH'' gene. Function Acyloxyacyl hydrolase (AOAH) is a lipase that selectively releases the secondary (acyloxyacyl-linked) fatty acyl chains from the hexaacyl lipid A moiety found in many bacterial lipopolysaccharide Lipopolysaccharides (LPS) are large molecules consisting of a lipid and a polysaccharide that are bacterial toxins. They are composed of an O-antigen, an outer core, and an inner core all joined by a covalent bond, and are found in the outer ...s (LPSs, also called endotoxins). The resulting tetraacyl LPS is non-stimulatory and can be a potent inhibitor of LPS sensing via the MD-2--Toll-like Receptor 4 (TLR4). The enzyme's 2 disulfide-linked subunits are encoded by a single mRNA. The smaller subunit is a member of the saposin-like (SAPLIP) protein family and the larger subunit, which contains the active site serine, is a GDSL lipase. The enzyme's 3D structure and c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Saposins
Prosaposin, also known as PSAP, is a protein which in humans is encoded by the ''PSAP'' gene. This highly conserved glycoprotein is a precursor for 4 cleavage products: saposins A, B, C, and D. Saposin is an acronym for Sphingolipid Activator PrO ''SeINs. Each domain of the precursor protein is approximately 80 amino acid residues long with nearly identical placement of cysteine residues and glycosylation sites. Saposins A-D localize primarily to the lysosomal compartment where they facilitate the catabolism of glycosphingolipids with short oligosaccharide groups. The precursor protein exists both as a secretory protein and as an integral membrane protein and has neurotrophic activities. Saposins A–D are required for the hydrolysis of certain sphingolipids by specific lysosomal hydrolases. Family members * Saposin A was identified as an N-terminal domain in the prosaposin cDNA prior to its isolation. It is known to stimulate the enzymatic hydrolysis of 4-methylumbellifer ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pulmonary Surfactant-associated Protein B
Surfactant protein B is an essential lipid-associated protein found in pulmonary surfactant. Without it, the lung would not be able to inflate after a deep breath out. It rearranges lipid molecules in the fluid lining the lung so that tiny air sacs in the lung, called alveoli, can more easily inflate. Gene SP-B is encoded by ''SFTPB'', a single, 11425 nucleotide long gene on chromosome 2. Mutations in this gene are the basis for several of the lung conditions mentioned above. Both frameshift mutations and several single nucleotide polymorphisms (SNPs) have been found correlated to a variety of lung conditions. A frame shift mutation responsible for congenital alveolar proteinosis (CAP) was identified by Kattan et al. Many SNP's have been identified in relation to lung conditions. They have been correlated to severe influenza, neonatal respiratory distress syndrome, mechanical ventilation necessity, and more. Protein Surfactant protein B (SP-B) is a small protein, weighing ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Dimer
In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word ''dimer'' has roots meaning "two parts", '' di-'' + '' -mer''. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins. A protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO. Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity. The G protein-coupled cannabinoid receptors have the ability to form both homo- and heterodimers with several ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phytepsin
Phytepsin () is an enzyme. This enzyme catalyses the following chemical reaction : Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-Asp- and -Asp-Asp- bonds in 2S albumin from plant seeds This enzyme is present in barley grain and other plants. It is an aspartic protease with a plant-specific insert The plant-specific insert (PSI) or plant-specific sequence (PSS) is an independent domain, exclusively found in plants, consisting of approximately 100 residues, found on the C-terminal lobe on some aspartic proteases (AP) called phytepsins. The .... References External links * {{Portal bar, Biology, border=no EC 3.4.23 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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