Working on endocrine pharm right now, and wondering what the difference is, mainly between 17,20-lyase and 17a-hydroxylase.
A benzaldehyde lyase catalyzed intramolecular stereoselective Stetter reaction, that has not been observed in other ThDPβdependent enzymes known in nature, was reported in this work. A series of chromanβ4βone derivatives, important building blocks in pharmaceuticals products, were obtained in high yield (up to 99β%) and stereoselectivity (up to 99:1 e.r.).
Abstract
The reliable design and prediction of enzyme promiscuity to access transformations not observed in nature remains a longβstanding challenge. Herein, we present the first example of an intramolecular stereoselective Stetter reaction catalyzed by benzaldehyde lyase, guided by the rational structure screening of various ThDPβdependent enzymes using molecular dynamics (MD) simulations. After optimization, high productivity (up to 99β%) and stereoselectivity (up to 99:1 e.r.) for this novel enzyme function was achieved.
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Hyaluronic acid lyase, also known as hyaluronidase or "hyaluronidase for injection", is an enzyme that hydrolyzes hyaluronic acid.Hyaluronic acid lyase is a natural enzyme, which has hydrolysis effect on hyaluronic acid :(eliminate the injection at inappropriate sites, eliminate the mass caused by excessive injection of hyaluronic acid, the elimination rate is up to 90%).Mainly used to repair hyaluronic acid modeling failure.Hyaluronic acid lysozyme is a substance that dissolves hyaluronic acid. After cosmetic hyaluronic acid injection, the effect is not very good. Hyaluronic acid lysozyme can be dissolved within 48 hours, and then it can be filled with hyaluronic acid again.
Julien
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Journal of the American Chemical SocietyDOI: 10.1021/jacs.1c00581
Yilin Liu, Ilia G. Denisov, Stephen G. Sligar, and James R. Kincaid
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In cabamoyl phosphate synthetase I, 2 ATP is used. The first ATP is used to activate the bicarbonate for nucleophilic attack by ammonia. The second ATP is used to phosphorylate the carbamoyl group to activate it for nucleophilic attack by ornithine's amine group. (phosphate is a good leaving group because inorganic phosphate is resonance stabilised) In this manner, the high energy phosphoanhydride bonds of ATP is being used to couple endergonic reactions to make the overall reaction exergonic.
What I don't understand is how ATP hydrolysis propels the reaction forward. Doesn't ATP hydrolysis simply liberate the phosphoanhydride bond in the form of heat? How do enzymes like citrate lyase harvest the energy liberated by ATP hydrolysis? Isn't it a waste to just hydrolyse ATP?
Thanks for any help!
super confused and spent a while looking over the internet; but the enzyme does not use energy from ATP or GTP (uses energy stored in thioester bond); and it has the name synthase; so i was thinking lyaase...? but then I see lots of people saying ligase...
Journal of the American Chemical SocietyDOI: 10.1021/jacs.0c08585
Adrien Pagnier, Hao Yang, Richard J. Jodts, Christopher D. James, Eric M. Shepard, Stella Impano, William E. Broderick, Brian M. Hoffman, and Joan B. Broderick
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https://www.mdpi.com/1422-0067/20/24/6124/htm
by π·MarΓa Arnedo 1,β ,π·Ana Latorre-Pellicer 1,β ,π·Cristina Lucia-Campos 1,π·Marta Gil-Salvador 1,π·Rebeca AntoΓ±anzas-PerΓ©z 1,π·Paulino GΓ³mez-Puertas 2π·,π·Gloria Bueno-Lozano 3,π·Beatriz Puisac 1,* andπ·Juan PiΓ© 1,*π·
Abstract
: There are three human enzymes with HMG-CoA lyase activity that are able to synthesize ketone bodies in different subcellular compartments. The mitochondrial HMG-CoA lyase was the first to be described, and catalyzes the cleavage of 3-hydroxy-3-methylglutaryl CoA to acetoacetate and acetyl-CoA, the common final step in ketogenesis and leucine catabolism. This protein is mainly expressed in the liver and its function is metabolic, since it produces ketone bodies as energetic fuels when glucose levels are low. Another isoform is encoded by the same gene for the mitochondrial HMG-CoA lyase (HMGCL), but it is located in peroxisomes. The last HMG-CoA lyase to be described is encoded by a different gene, HMGCLL1, and is located in the cytosolic side of the endoplasmic reticulum membrane. Some activity assays and tissue distribution of this enzyme have shown the brain and lung as key tissues for studying its function. Although the roles of the peroxisomal and cytosolic HMG-CoA lyases remain unknown, recent studies highlight the role of ketone bodies in metabolic remodeling, homeostasis, and signaling, providing new insights into the molecular and cellular function of these enzymes.
Keywords: HMG-CoA lyase; HMGCL; HMGCLL1; ketone bodies; 3-hydroxy-3-methylglutaric aciduria
https://preview.redd.it/i2l77sffv9k41.png?width=3663&format=png&auto=webp&s=66e4
... keep reading on reddit β‘How can we classify it using systematic nomenclature?
