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SCO1
Protein SCO1 homolog, mitochondrial, also known as SCO1, cytochrome c oxidase assembly protein, is a protein that in humans is encoded by the ''SCO1'' gene. SCO1 localizes predominantly to blood vessels, whereas SCO2 is barely detectable, as well as to tissues with high levels of oxidative phosphorylation. The expression of SCO2 is also much higher than that of SCO1 in muscle tissue, while SCO1 is expressed at higher levels in liver tissue than SCO2. Mutations in both ''SCO1'' and '' SCO2'' are associated with distinct clinical phenotypes as well as tissue-specific cytochrome c oxidase (complex IV) deficiency. Structure ''SCO1'' is located on the p arm of chromosome 17 in position 13.1 and has 6 exons. The ''SCO1'' gene produces a 33.8 kDa protein composed of 301 amino acids. The protein is a member of the SCO1/2 family. It contains 3 copper metal binding sites at positions 169, 173, and 260, a transit peptide, a 25 amino acid topological domain from positions 68–92, a 19 a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SCO2
SCO2 cytochrome c oxidase assembly (also known as SCO2 homolog, mitochondrial and SCO cytochrome oxidase deficient homolog 2) is a protein that in humans is encoded by the ''SCO2'' gene. The encoded protein is one of the cytochrome c oxidase (COX)(Complex IV) assembly factors. Human COX is a multimeric protein complex that requires several assembly factors. Cytochrome c oxidase (COX) catalyzes the transfer of electrons from cytochrome c to molecular oxygen, which helps to maintain the proton gradient across the inner mitochondrial membrane that is necessary for aerobic ATP production. The encoded protein is a metallochaperone that is involved in the biogenesis of cytochrome c oxidase subunit II. Mutations in this gene are associated with fatal infantile encephalocardiomyopathy and myopia 6. Structure The ''SCO2'' gene is located on the q arm of chromosome 22 at position 13.33 and it spans 2,871 base pairs. The ''SCO2'' gene produces a 15.1 kDa protein composed of 136 amino ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome C Oxidase
The enzyme cytochrome c oxidase or Complex IV (was , now reclassified as a translocasEC 7.1.1.9 is a large transmembrane protein complex found in bacteria, archaea, and the mitochondria of eukaryotes. It is the last enzyme in the Cellular respiration, respiratory electron transport chain of cell (biology), cells located in the membrane. It receives an electron from each of four cytochrome c molecules and transfers them to one oxygen molecule and four protons, producing two molecules of water. In addition to binding the four protons from the inner aqueous phase, it transports another four protons across the membrane, increasing the transmembrane difference of proton electrochemical potential, which the ATP synthase then uses to synthesize Adenosine triphosphate, ATP. Structure The complex The complex is a large integral membrane protein composed of several Cofactor (biochemistry)#Metal ions, metal prosthetic sites and 13 protein subunits in mammals. In mammals, ten subunits a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Alpha Helix
An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the Protein secondary structure, secondary structure of proteins. It is also the most extreme type of local structure, and it is the local structure that is most easily predicted from a sequence of amino acids. The alpha helix has a right-handed helix conformation in which every backbone amino, N−H group hydrogen bonds to the backbone carbonyl, C=O group of the amino acid that is four residue (biochemistry), residues earlier in the protein sequence. Other names The alpha helix is also commonly called a: * Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure) * 3.613-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen) Discovery ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Homeostasis
In biology, homeostasis (British English, British also homoeostasis; ) is the state of steady internal physics, physical and chemistry, chemical conditions maintained by organism, living systems. This is the condition of optimal functioning for the organism and includes many variables, such as body temperature and fluid balance, being kept within certain pre-set limits (homeostatic range). Other variables include the pH of extracellular fluid, the concentrations of sodium, potassium, and calcium ions, as well as the blood sugar level, and these need to be regulated despite changes in the environment, diet, or level of activity. Each of these variables is controlled by one or more regulators or homeostatic mechanisms, which together maintain life. Homeostasis is brought about by a natural resistance to change when already in optimal conditions, and equilibrium is maintained by many regulatory mechanisms; it is thought to be the central motivation for all organic action. All home ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome C Oxidase Subunit II
Cytochrome c oxidase II is a protein in eukaryotes that is encoded by the MT-CO2 gene. Cytochrome c oxidase subunit II, abbreviated COXII, COX2, COII, or MT-CO2, is the second subunit of cytochrome c oxidase. It is also one of the three mitochondrial DNA (mtDNA) encoded subunits ( MT-CO1, MT-CO2, MT-CO3) of respiratory complex IV. Structure In humans, the ''MT-CO2'' gene is located on the p arm of mitochondrial DNA at position 12 and it spans 683 base pairs. The ''MT-CO2'' gene produces a 25.6 kDa protein composed of 227 amino acids. MT-CO2 is a subunit of the enzyme Cytochrome c oxidase () (Complex IV), an oligomeric enzymatic complex of the mitochondrial respiratory chain involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane. The enzyme complex consists of 3-4 subunits (prokaryotes) to up to 13 polypept ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Metallochaperone
Metallochaperones are a distinct class of molecular chaperones that facilitate the intracellular transport of metal ions to different metalloproteins, e.g., metalloenzymes, in cells through specific protein-protein interactions. In this way, for example, the proteins ensure that the correct metal ion cofactor is acquired by its corresponding metalloenzyme. Metallochaperones are essential to the proper functioning of cells, playing a vital role in a large number of biological processes including, for example, respiration, photosynthesis, neurotransmission, and protein folding. Prior to the discovery of metallochaperones in the late 1990s, biologists believed that metal ions freely diffused within cells without the aid of auxiliary proteins. Today, it is well established that these special molecules contribute to the intracellular homeostatic control of biometal ion An ion () is an atom or molecule with a net electrical charge. The charge of an electron is considered to be ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Brain
The brain is an organ (biology), organ that serves as the center of the nervous system in all vertebrate and most invertebrate animals. It consists of nervous tissue and is typically located in the head (cephalization), usually near organs for special senses such as visual perception, vision, hearing, and olfaction. Being the most specialized organ, it is responsible for receiving information from the sensory nervous system, processing that information (thought, cognition, and intelligence) and the coordination of motor control (muscle activity and endocrine system). While invertebrate brains arise from paired segmental ganglia (each of which is only responsible for the respective segmentation (biology), body segment) of the ventral nerve cord, vertebrate brains develop axially from the midline dorsal nerve cord as a brain vesicle, vesicular enlargement at the rostral (anatomical term), rostral end of the neural tube, with centralized control over all body segments. All vertebr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heart
The heart is a muscular Organ (biology), organ found in humans and other animals. This organ pumps blood through the blood vessels. The heart and blood vessels together make the circulatory system. The pumped blood carries oxygen and nutrients to the tissue, while carrying metabolic waste such as carbon dioxide to the lungs. In humans, the heart is approximately the size of a closed fist and is located between the lungs, in the middle compartment of the thorax, chest, called the mediastinum. In humans, the heart is divided into four chambers: upper left and right Atrium (heart), atria and lower left and right Ventricle (heart), ventricles. Commonly, the right atrium and ventricle are referred together as the right heart and their left counterparts as the left heart. In a healthy heart, blood flows one way through the heart due to heart valves, which prevent cardiac regurgitation, backflow. The heart is enclosed in a protective sac, the pericardium, which also contains a sma ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Homology (biology)
In biology, homology is similarity in anatomical structures or genes between organisms of different taxa due to shared ancestry, ''regardless'' of current functional differences. Evolutionary biology explains homologous structures as retained heredity from a common descent, common ancestor after having been subjected to adaptation (biology), adaptive modifications for different purposes as the result of natural selection. The term was first applied to biology in a non-evolutionary context by the anatomist Richard Owen in 1843. Homology was later explained by Charles Darwin's theory of evolution in 1859, but had been observed before this from Aristotle's biology onwards, and it was explicitly analysed by Pierre Belon in 1555. A common example of homologous structures is the forelimbs of vertebrates, where the bat wing development, wings of bats and origin of avian flight, birds, the arms of primates, the front flipper (anatomy), flippers of whales, and the forelegs of quadrupedalis ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Holoprotein
A holoprotein or conjugated protein is an apoprotein combined with its prosthetic group. Some enzymes do not need additional components to show full activity. Others require non-protein molecules called cofactors to be bound for activity. Cofactors can be either inorganic (e.g., metal ions and iron-sulfur clusters) or organic compounds (e.g., flavin and heme). Organic cofactors can be either coenzymes, which are released from the enzyme's active site during the reaction, or prosthetic groups, which are tightly bound to an enzyme. Organic prosthetic groups can be covalently bound (e.g., biotin in enzymes such as pyruvate carboxylase). An example of an enzyme that contains a cofactor is carbonic anhydrase, which has a zinc cofactor bound as part of its active site. These tightly bound ions or molecules are usually found in the active site and are involved in catalysis. For example, flavin and heme cofactors are often involved in redox reactions. Enzymes that require a cofactor ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Yeast
Yeasts are eukaryotic, single-celled microorganisms classified as members of the fungus kingdom (biology), kingdom. The first yeast originated hundreds of millions of years ago, and at least 1,500 species are currently recognized. They are estimated to constitute 1% of all described fungal species. Some yeast species have the ability to develop multicellular characteristics by forming strings of connected budding cells known as pseudohyphae or false hyphae, or quickly evolve into a Multicellular organism, multicellular cluster with specialised Organelle, cell organelles function. Yeast sizes vary greatly, depending on species and environment, typically measuring 3–4 micrometre, μm in diameter, although some yeasts can grow to 40 μm in size. Most yeasts reproduce asexual reproduction, asexually by mitosis, and many do so by the asymmetric division process known as budding. With their single-celled growth habit, yeasts can be contrasted with Mold (fungus), molds, wh ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
