Utp full form in biochemistry

E. coli Aspartate Transcarbamoylase (ATCase) Allen Sanderlin '15 and Kaitlin Creamer '16 Contents: I. Introduction Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that L-aspartate and carbamoyl phosphate (CP) to produce N-carbamoyl- L-aspartate (CAA). This reaction is the first committed step of the Cytidine triphosphate ( In mammals, ATCase forms part of the multi-enzyme complex CAD (alongside carbamoyl phosphate synthetase II and dihydroorotase) that catalyzes several steps in pyrimidine biosynthesis. Since pyrimidines are essential for DNA synthesis during cell division, ATCase inhibitors such as the transition-state analogue N-(phosphonacetyl)- L-aspartate ( Allosteric regulation of ATCase by CTP and UTP prevents a pyrimidine surplus. These effectors synergistically inhibit ATCase activity, establishing a negative feedback loop. Conversely, adenosine triphosphate ( II. General Structure The Escherichia coli ATCase is a 310 kDa dodecamer consisting of two catalytic homotrimers and three regulatory homodimers encoded by pyrB and pyrI, respectively. The interfaces between adjacent catalytic subunits form six active sites for binding of CP and L-aspartate regulatory subunits form six allosteric sites for NTP binding regulatory subunit contains a zinc-binding domain that is necessary for assembly of the complex. Within this domain, a Zn 2+ cation is tetrahedrally coordinated to Cys109, Cys114, Cys138, and Cys141 catalytic subunit contains eleven parallel beta she...

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Cytidine Triphosphate Cytidine triphosphate (CTP) is an allosteric inhibitor representing a classic case of feedback inhibition whereby the end product of a biosynthetic pathway inhibits an enzyme catalyzing a reaction at the beginning of the pathway. From: Encyclopedia of Biological Chemistry (Second Edition), 2013 Related terms: • Choline • Anabolism • Phosphatidylcholine • Lysozyme • Cytidine Diphosphate • Synthase • Phosphate • Diacylglycerol • RNA • Glutamine Cytidine triphosphate synthetase (CTPS) mediates the conversion of uridine triphosphate (UTP) into cytidine triphosphate (CTP) ( Scheme 17), which is the rate-limiting step of de novo CTP biosynthesis. 46,178 As a consequence, CTPS activity regulates the intracellular rates of RNA, DNA, and phospholipid synthesis. 179,180 This enzyme has therefore been selected as a target for the development of drugs against leukemia 181 and parasitic infections, 182,183 and its kinetic properties have been the subject of numerous studies. 184–187 GTP is an allosteric activator of CTPS, 188 and GTP binding enhances the utilization of ammonia released in the glutaminase domain of the CTPS in Lactococcus lactis. 189 Enzyme activity is downregulated by CTP, which competes with UTP for binding to the synthetase site, 190 and there is evidence that phosphorylation at a number of serine residues is an important mechanism for the regulation of both the human and yeast CTP synthetases. 191,192 Substrate-induced changes in CTPS oligomeri...

Human UTP—glucose-1-phosphate uridylyltransferase cartoon created in pymol Identifiers Databases Search UTP—glucose-1-phosphate uridylyltransferase also known as glucose-1-phosphate uridylyltransferase (or UDP–glucose pyrophosphorylase) is an enzyme involved in ⇌ UTP—glucose-1-phosphate uridylyltransferase is an enzyme found in all three Structure [ ] The structure of UTP—glucose-1-phosphate uridylyltransferase is significantly different between In humans, each enzyme subunit contains several residues (L113, N251, and N328) that are highly conserved in eukaryotes. A • UDP-glucose pyrophosphorylase 1, homooctamer, Human Identifiers Symbol UGP1 Other data UDP–glucose pyrophosphorylase 2 Identifiers Symbol UGP2 Other data Search for Structures Domains Function [ ] UTP—glucose-1-phosphate uridylyltransferase is ubiquitous in nature due to its important role in the generation of In higher animals, the enzyme is highly active in tissues involved in UTP—glucose-1-phosphate uridylyltransferase is also required for Mechanism [ ] In this enzyme's primary reaction, the phosphate group on UTP—glucose-1-phosphate uridylyltransferase uses an Similar to other sugar 2+ ion is coordinated by a phosphoryl oxygen on glucose 1-phosphate and by an α-phosphoryl oxygen on UTP. 2+ is thought to orient the glucose 1-phosphate for Regulation [ ] Although functionally similar across species, UDP-glucose pyrophosphorylase has different structures and regulation mechanisms in different organisms. Mic...

Chapter 27 Chapter 27 from: Heidi/chapter27/chp27.htm The Synthesis and Degradation of Nucleotides Pigeon drinking at Gaia Fountain, Siena, Italy. The basic features of purine biosyn- thesis were elucidated initially from metabolic studies of nitrogen metabolism in pigeons. Pigeons excrete excess N as uric acid, a purine analog. (Arte & Imamagini srl/Corbis Images.) N ucleotides are ubiquitous constituents of life, actively participating in the majority of biochemical reactions. Recall that ATP is the “energy currency” of the cell, that uridine nucleotide derivatives of carbohydrates are common intermediates in cellular transformations of carbohydrates ( 27.1 · Nucleotide Biosynthesis Nearly all organisms can make the purine and pyrimidine nucleotides via so-called de novo biosynthetic pathways. (De novo means “anew”; a less literal but more apt translation might be “from scratch” because de novo pathways are metabolic sequences that form complex end products from rather simple precursors.) Many organisms also have salvage pathways to recover purine and pyrimidine compounds obtained in the diet or released during nucleic acid turnover and degradation. While the ribose of nucleotides can be catabolized to generate energy, the nitrogenous bases do not serve as energy sources; their catabolism does not lead to products used by pathways of energy conservation. Compared to slowly dividing cells, rapidly proliferating cells synthesize larger amounts of DNA and RNA per unit time....

Term Definition Rating Unshielded Twisted Pair Rate it: Unshielded Twisted Pairs Rate it: Unsheilded Twisted Pair Rate it: Utapao, Thailand Rate it: U Twisted Pair Rate it: Unshileded Twisted Pair Rate it: Universal Transmission Protocol Rate it: Unlisted Trading Privileges Company Rate it: Unknown Twisted Pair Rate it: Universal Transfer Protocol Rate it: A Universal Time Protocol Rate it: Uncertain Tax Position Rate it: Unifying Theories of Programming Rate it: University of Toronto Press Rate it: Up The Pooper Rate it: Universal Transport Packet Rate it: Universidad Tecnológica de Panamá Rate it: Use Transcriber Preference Rate it: Up Town Projects Rate it: Untwisted Transmission Pairs Rate it: Urban Technology Project Rate it: Urban Theatre Projects Rate it: Urban Transit Program Rate it: Unshielded Transmission Protocol Rate it: Used Tractor Parts Rate it:

E. coli Aspartate Transcarbamoylase (ATCase) Allen Sanderlin '15 and Kaitlin Creamer '16 Contents: I. Introduction Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that L-aspartate and carbamoyl phosphate (CP) to produce N-carbamoyl- L-aspartate (CAA). This reaction is the first committed step of the Cytidine triphosphate ( In mammals, ATCase forms part of the multi-enzyme complex CAD (alongside carbamoyl phosphate synthetase II and dihydroorotase) that catalyzes several steps in pyrimidine biosynthesis. Since pyrimidines are essential for DNA synthesis during cell division, ATCase inhibitors such as the transition-state analogue N-(phosphonacetyl)- L-aspartate ( Allosteric regulation of ATCase by CTP and UTP prevents a pyrimidine surplus. These effectors synergistically inhibit ATCase activity, establishing a negative feedback loop. Conversely, adenosine triphosphate ( II. General Structure The Escherichia coli ATCase is a 310 kDa dodecamer consisting of two catalytic homotrimers and three regulatory homodimers encoded by pyrB and pyrI, respectively. The interfaces between adjacent catalytic subunits form six active sites for binding of CP and L-aspartate regulatory subunits form six allosteric sites for NTP binding regulatory subunit contains a zinc-binding domain that is necessary for assembly of the complex. Within this domain, a Zn 2+ cation is tetrahedrally coordinated to Cys109, Cys114, Cys138, and Cys141 catalytic subunit contains eleven parallel beta she...

Chapter 27 Chapter 27 from: Heidi/chapter27/chp27.htm The Synthesis and Degradation of Nucleotides Pigeon drinking at Gaia Fountain, Siena, Italy. The basic features of purine biosyn- thesis were elucidated initially from metabolic studies of nitrogen metabolism in pigeons. Pigeons excrete excess N as uric acid, a purine analog. (Arte & Imamagini srl/Corbis Images.) N ucleotides are ubiquitous constituents of life, actively participating in the majority of biochemical reactions. Recall that ATP is the “energy currency” of the cell, that uridine nucleotide derivatives of carbohydrates are common intermediates in cellular transformations of carbohydrates ( 27.1 · Nucleotide Biosynthesis Nearly all organisms can make the purine and pyrimidine nucleotides via so-called de novo biosynthetic pathways. (De novo means “anew”; a less literal but more apt translation might be “from scratch” because de novo pathways are metabolic sequences that form complex end products from rather simple precursors.) Many organisms also have salvage pathways to recover purine and pyrimidine compounds obtained in the diet or released during nucleic acid turnover and degradation. While the ribose of nucleotides can be catabolized to generate energy, the nitrogenous bases do not serve as energy sources; their catabolism does not lead to products used by pathways of energy conservation. Compared to slowly dividing cells, rapidly proliferating cells synthesize larger amounts of DNA and RNA per unit time....

Human UTP—glucose-1-phosphate uridylyltransferase cartoon created in pymol Identifiers Databases Search UTP—glucose-1-phosphate uridylyltransferase also known as glucose-1-phosphate uridylyltransferase (or UDP–glucose pyrophosphorylase) is an enzyme involved in ⇌ UTP—glucose-1-phosphate uridylyltransferase is an enzyme found in all three Structure [ ] The structure of UTP—glucose-1-phosphate uridylyltransferase is significantly different between In humans, each enzyme subunit contains several residues (L113, N251, and N328) that are highly conserved in eukaryotes. A • UDP-glucose pyrophosphorylase 1, homooctamer, Human Identifiers Symbol UGP1 Other data UDP–glucose pyrophosphorylase 2 Identifiers Symbol UGP2 Other data Search for Structures Domains Function [ ] UTP—glucose-1-phosphate uridylyltransferase is ubiquitous in nature due to its important role in the generation of In higher animals, the enzyme is highly active in tissues involved in UTP—glucose-1-phosphate uridylyltransferase is also required for Mechanism [ ] In this enzyme's primary reaction, the phosphate group on UTP—glucose-1-phosphate uridylyltransferase uses an Similar to other sugar 2+ ion is coordinated by a phosphoryl oxygen on glucose 1-phosphate and by an α-phosphoryl oxygen on UTP. 2+ is thought to orient the glucose 1-phosphate for Regulation [ ] Although functionally similar across species, UDP-glucose pyrophosphorylase has different structures and regulation mechanisms in different organisms. Mic...

Cytidine Triphosphate Cytidine triphosphate (CTP) is an allosteric inhibitor representing a classic case of feedback inhibition whereby the end product of a biosynthetic pathway inhibits an enzyme catalyzing a reaction at the beginning of the pathway. From: Encyclopedia of Biological Chemistry (Second Edition), 2013 Related terms: • Choline • Anabolism • Phosphatidylcholine • Lysozyme • Cytidine Diphosphate • Synthase • Phosphate • Diacylglycerol • RNA • Glutamine Cytidine triphosphate synthetase (CTPS) mediates the conversion of uridine triphosphate (UTP) into cytidine triphosphate (CTP) ( Scheme 17), which is the rate-limiting step of de novo CTP biosynthesis. 46,178 As a consequence, CTPS activity regulates the intracellular rates of RNA, DNA, and phospholipid synthesis. 179,180 This enzyme has therefore been selected as a target for the development of drugs against leukemia 181 and parasitic infections, 182,183 and its kinetic properties have been the subject of numerous studies. 184–187 GTP is an allosteric activator of CTPS, 188 and GTP binding enhances the utilization of ammonia released in the glutaminase domain of the CTPS in Lactococcus lactis. 189 Enzyme activity is downregulated by CTP, which competes with UTP for binding to the synthetase site, 190 and there is evidence that phosphorylation at a number of serine residues is an important mechanism for the regulation of both the human and yeast CTP synthetases. 191,192 Substrate-induced changes in CTPS oligomeri...