Category: Aminosaurs
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The conjugate (10S,11S) JH diol phosphate is the product of a two-step enzymatic process: conversion of JH to JH diol and then addition of a phosphate group to C10
The conjugate (10S,11S) JH diol phosphate is the product of a two-step enzymatic process: conversion of JH to JH diol and then addition of a phosphate group to C10. The enzyme responsible for the phosphorylation of JH diol is JH diol kinase (JHDK), which was first characterized from the Malpighian tubules of early fifth instars of M. sexta. The Malpighian tubule system is a type of excretory and osmoregulatory system found in…
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The Yolk’s On Us: Unraveling the Secrets of Vitellogenesis
Hold onto your ovaries, folks! We’re about to dive into the wild world of Vitellogenesis – the cellular rave where eggs get their groove on! Picture this: You’re a lonely liver cell, minding your own business, when suddenly – BAM! – you’re hit with a tsunami of estradiol. It’s like Mother Nature’s Red Bull, and…
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The PVN Powerhouse: How the Paraventricular Nucleus Rules Hormone Secretion
Hold onto your hypothalamus, folks! We’re about to dive into the wild world of the Paraventricular Nucleus (PVN), where tiny cells pack a mighty hormonal punch! Picture this: deep in the brain’s control center, the hypothalamus, sits the PVN – a cluster of cells that’s like the body’s own hormone factory. But we’re not talking…
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Vitellin is essential in the fertilization process, and embryonic development in egg-laying organisms
Vitellin is a protein found in the egg yolk. It is a phosphoprotein. Vitellin is a generic name for major of many yolk proteins. Vitellin has been known since the 1900s. The periodic acid-Schiff method and Sudan black B dye was used to help determine that Vitellin is a glycolipoprotein because it stained positive when tested. This protein was…
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Protein phosphorylation was first reported in 1906
Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become activated, deactivated, or otherwise modifying its function. Approximately 13,000 human proteins have sites that are phosphorylated. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by…
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Phosphorylation
In biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion.[1] This process and its inverse, dephosphorylation, are common in biology.[2] Protein phosphorylation often activates (or deactivates) many enzymes.[3][4] During respiration and photosynthesis Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the “high-energy” exchange medium in the cell. During aerobic respiration, ATP is synthesized…
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Ku is a dimeric protein complex that binds to DNA double-strand break ends and is required for the non-homologous end joining (NHEJ) pathway of DNA repair
Ku is evolutionarily conserved from bacteria to humans. The ancestral bacterial Ku is a homodimer (two copies of the same protein bound to each other).[2] Eukaryotic Ku is a heterodimer of two polypeptides, Ku70 (XRCC6) and Ku80 (XRCC5), so named because the molecular weight of the human Ku proteins is around 70 kDa and 80 kDa. The two Ku subunits form a basket-shaped structure that threads onto…
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Ku70
Ku70 is a protein that, in humans, is encoded by the XRCC6 gene.[5][6] Function Together, Ku70 and Ku80 make up the Ku heterodimer, which binds to DNA double-strand break ends and is required for the non-homologous end joining (NHEJ) pathway of DNA repair. It is also required for V(D)J recombination, which utilizes the NHEJ pathway to promote antigen diversity in the mammalian immune system. In addition to its role in NHEJ, Ku…
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Ku80
Ku80 is a protein that, in humans, is encoded by the XRCC5 gene.[5] Together, Ku70 and Ku80 make up the Ku heterodimer, which binds to DNA double-strand break ends and is required for the non-homologous end joining (NHEJ) pathway of DNA repair. It is also required for V(D)J recombination, which utilizes the NHEJ pathway to promote antigen diversity in the mammalian immune system. In addition to its role in NHEJ, Ku is required…
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The trefoil knot fold is a protein fold in which the protein backbone is twisted into a trefoil knot shape
“Shallow” knots in which the tail of the polypeptide chain only passes through a loop by a few residues are uncommon, but “deep” knots in which many residues are passed through the loop are extremely rare. Deep trefoil knots have been found in the SPOUT superfamily. including methyltransferase proteins involved in posttranscriptional RNA modification in all three domains of life, including bacterium Thermus thermophilus and…
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Cyanamide notes (it was a polio vaccine that spurred these notes and by now polio has five mentions on the page and these are two of them)
I’m going to add some polio vaccine stuff at the top of these notes. Hilary Koprowski is the one mentioned on the Polio Hall of Fame page who was not included in the hideous monument, see What In God’s Name, even though he (and his work) have direct connection to those who are included. He…
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Aliivibrio fischeri (aka Vibrio fischeri), a bioluminescent bacteria and a glowing squid
Aliivibrio fischeri (also called Vibrio fischeri) is a Gram-negative, rod-shaped bacterium found globally in marine environments. This species has bioluminescent properties, and is found predominantly in symbiosis with various marine animals, such as the Hawaiian bobtail squid. It is heterotrophic, oxidase-positive, and motile by means of a single polar flagella. Free-living A. fischeri cells survive on decaying organic matter. The bacterium is a key research organism for examination of microbial bioluminescence, quorum sensing, and bacterial-animal symbiosis. It is named…
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Tracheal cytotoxin (TCT) is a soluble piece of peptidoglycan (PGN) found in the cell wall of all gram-negative bacteria, but only some bacteria species release TCT including Bordetella pertussis, Vibrio fischeri, and Neisseria gonorrhoeae
Tracheal cytotoxin (TCT) is a 921 dalton glycopeptide released by Bordetella pertussis, Vibrio fischeri (as a symbiosis chemical), and Neisseria gonorrhoeae (among other peptidoglycan-derived cytotoxins it produces). It is a soluble piece of peptidoglycan (PGN) found in the cell wall of all gram-negative bacteria, but only some bacteria species release TCT due to inability to recycle this piece of anhydromuropeptide. History In 1980, it was discovered that B. pertussis could attach to hamster tracheal epithelial (HTE) cells, and also, that…
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Fibroin is an insoluble protein present in silk produced by numerous insects
Fibroin is an insoluble protein present in silk produced by numerous insects, such as the larvae of Bombyx mori, and other moth genera such as Antheraea, Cricula, Samia and Gonometa. Silk in its raw state consists of two main proteins, sericin and fibroin, with a glue-like layer of sericin coating two singular filaments of fibroin called brins. BRIN AND BAVE (BRIN) One of the radiating sticks of a fan.…
