Journal articles: 'Enzyme function'

1

Dunaway-Mariano, Debra. "Enzyme Function Discovery." Structure 16, no. 11 (November 2008): 1599–600. http://dx.doi.org/10.1016/j.str.2008.10.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Tan, Yong Quan, Bo Xue, and Wen Shan Yew. "Genetically Encodable Scaffolds for Optimizing Enzyme Function." Molecules 26, no. 5 (March 4, 2021): 1389. http://dx.doi.org/10.3390/molecules26051389.

Full text

Abstract:

Enzyme engineering is an indispensable tool in the field of synthetic biology, where enzymes are challenged to carry out novel or improved functions. Achieving these goals sometimes goes beyond modifying the primary sequence of the enzyme itself. The use of protein or nucleic acid scaffolds to enhance enzyme properties has been reported for applications such as microbial production of chemicals, biosensor development and bioremediation. Key advantages of using these assemblies include optimizing reaction conditions, improving metabolic flux and increasing enzyme stability. This review summarizes recent trends in utilizing genetically encodable scaffolds, developed in line with synthetic biology methodologies, to complement the purposeful deployment of enzymes. Current molecular tools for constructing these synthetic enzyme-scaffold systems are also highlighted.

APA, Harvard, Vancouver, ISO, and other styles

3

Gerlt, John A., Karen N. Allen, Steven C. Almo, Richard N. Armstrong, Patricia C. Babbitt, John E. Cronan, Debra Dunaway-Mariano, et al. "The Enzyme Function Initiative." Biochemistry 50, no. 46 (November 22, 2011): 9950–62. http://dx.doi.org/10.1021/bi201312u.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Romero, Philip A., Tuan M. Tran, and Adam R. Abate. "Dissecting enzyme function with microfluidic-based deep mutational scanning." Proceedings of the National Academy of Sciences 112, no. 23 (May 26, 2015): 7159–64. http://dx.doi.org/10.1073/pnas.1422285112.

Full text

Abstract:

Natural enzymes are incredibly proficient catalysts, but engineering them to have new or improved functions is challenging due to the complexity of how an enzyme’s sequence relates to its biochemical properties. Here, we present an ultrahigh-throughput method for mapping enzyme sequence–function relationships that combines droplet microfluidic screening with next-generation DNA sequencing. We apply our method to map the activity of millions of glycosidase sequence variants. Microfluidic-based deep mutational scanning provides a comprehensive and unbiased view of the enzyme function landscape. The mapping displays expected patterns of mutational tolerance and a strong correspondence to sequence variation within the enzyme family, but also reveals previously unreported sites that are crucial for glycosidase function. We modified the screening protocol to include a high-temperature incubation step, and the resulting thermotolerance landscape allowed the discovery of mutations that enhance enzyme thermostability. Droplet microfluidics provides a general platform for enzyme screening that, when combined with DNA-sequencing technologies, enables high-throughput mapping of enzyme sequence space.

APA, Harvard, Vancouver, ISO, and other styles

5

Page, Michael J., and Enrico Di Cera. "Role of Na+and K+in Enzyme Function." Physiological Reviews 86, no. 4 (October 2006): 1049–92. http://dx.doi.org/10.1152/physrev.00008.2006.

Full text

Abstract:

Metal complexation is a key mediator or modifier of enzyme structure and function. In addition to divalent and polyvalent metals, group IA metals Na+and K+play important and specific roles that assist function of biological macromolecules. We examine the diversity of monovalent cation (M+)-activated enzymes by first comparing coordination in small molecules followed by a discussion of theoretical and practical aspects. Select examples of enzymes that utilize M+as a cofactor (type I) or allosteric effector (type II) illustrate the structural basis of activation by Na+and K+, along with unexpected connections with ion transporters. Kinetic expressions are derived for the analysis of type I and type II activation. In conclusion, we address evolutionary implications of Na+binding in the trypsin-like proteases of vertebrate blood coagulation. From this analysis, M+complexation has the potential to be an efficient regulator of enzyme catalysis and stability and offers novel strategies for protein engineering to improve enzyme function.

APA, Harvard, Vancouver, ISO, and other styles

6

Duskey, Jason Thomas, Federica da Ros, Ilaria Ottonelli, Barbara Zambelli, Maria Angela Vandelli, Giovanni Tosi, and Barbara Ruozi. "Enzyme Stability in Nanoparticle Preparations Part 1: Bovine Serum Albumin Improves Enzyme Function." Molecules 25, no. 20 (October 9, 2020): 4593. http://dx.doi.org/10.3390/molecules25204593.

Full text

Abstract:

Enzymes have gained attention for their role in numerous disease states, calling for research for their efficient delivery. Loading enzymes into polymeric nanoparticles to improve biodistribution, stability, and targeting in vivo has led the field with promising results, but these enzymes still suffer from a degradation effect during the formulation process that leads to lower kinetics and specific activity leading to a loss of therapeutic potential. Stabilizers, such as bovine serum albumin (BSA), can be beneficial, but the knowledge and understanding of their interaction with enzymes are not fully elucidated. To this end, the interaction of BSA with a model enzyme B-Glu, part of the hydrolase class and linked to Gaucher disease, was analyzed. To quantify the natural interaction of beta-glucosidase (B-Glu,) and BSA in solution, isothermal titration calorimetry (ITC) analysis was performed. Afterwards, polymeric nanoparticles encapsulating these complexes were fully characterized, and the encapsulation efficiency, activity of the encapsulated enzyme, and release kinetics of the enzyme were compared. ITC results showed that a natural binding of 1:1 was seen between B-Glu and BSA. Complex concentrations did not affect nanoparticle characteristics which maintained a size between 250 and 350 nm, but increased loading capacity (from 6% to 30%), enzyme activity, and extended-release kinetics (from less than one day to six days) were observed for particles containing higher B-Glu:BSA ratios. These results highlight the importance of understanding enzyme:stabilizer interactions in various nanoparticle systems to improve not only enzyme activity but also biodistribution and release kinetics for improved therapeutic effects. These results will be critical to fully characterize and compare the effect of stabilizers, such as BSA with other, more relevant therapeutic enzymes for central nervous system (CNS) disease treatments.

APA, Harvard, Vancouver, ISO, and other styles

7

BORMAN, STU. "PROBING ENZYME FUNCTION IN CELLS." Chemical & Engineering News 84, no. 44 (October 30, 2006): 12. http://dx.doi.org/10.1021/cen-v084n044.p012a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Mitchell, John BO. "Enzyme function and its evolution." Current Opinion in Structural Biology 47 (December 2017): 151–56. http://dx.doi.org/10.1016/j.sbi.2017.10.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Crunkhorn, Sarah. "Enzyme inhibitor improves cognitive function." Nature Reviews Drug Discovery 13, no. 10 (September 19, 2014): 726. http://dx.doi.org/10.1038/nrd4452.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Poulos, Thomas L. "Heme Enzyme Structure and Function." Chemical Reviews 114, no. 7 (January 8, 2014): 3919–62. http://dx.doi.org/10.1021/cr400415k.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Zhang, Wen, and Tao Pan. "A dual function PUS enzyme." Nature Chemical Biology 16, no. 2 (January 23, 2020): 107–8. http://dx.doi.org/10.1038/s41589-019-0450-z.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

GUPTA, Munishwar N. "Enzyme function in organic solvents." European Journal of Biochemistry 203, no. 1-2 (January 1992): 25–32. http://dx.doi.org/10.1111/j.1432-1033.1992.tb19823.x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Latip, Wahhida, Victor Feizal Knight, Norhana Abdul Halim, Keat Khim Ong, Noor Azilah Mohd Kassim, Wan Md Zin Wan Yunus, Siti Aminah Mohd Noor, and Mohd Shukuri Mohamad Ali. "Microbial Phosphotriesterase: Structure, Function, and Biotechnological Applications." Catalysts 9, no. 8 (August 7, 2019): 671. http://dx.doi.org/10.3390/catal9080671.

Full text

Abstract:

The role of phosphotriesterase as an enzyme which is able to hydrolyze organophosphate compounds cannot be disputed. Contamination by organophosphate (OP) compounds in the environment is alarming, and even more worrying is the toxicity of this compound, which affects the nervous system. Thus, it is important to find a safer way to detoxify, detect and recuperate from the toxicity effects of this compound. Phosphotriesterases (PTEs) are mostly isolated from soil bacteria and are classified as metalloenzymes or metal-dependent enzymes that contain bimetals at the active site. There are three separate pockets to accommodate the substrate into the active site of each PTE. This enzyme generally shows a high catalytic activity towards phosphotriesters. These microbial enzymes are robust and easy to manipulate. Currently, PTEs are widely studied for the detection, detoxification, and enzyme therapies for OP compound poisoning incidents. The discovery and understanding of PTEs would pave ways for greener approaches in biotechnological applications and to solve environmental issues relating to OP contamination.

APA, Harvard, Vancouver, ISO, and other styles

14

Sher, Hassan, Hazrat Ali, Muhammad H. Rashid, Fariha Iftikhar, Saif-ur-Rehman, Muhammad S. Nawaz, and Waheed S. Khan. "Enzyme Immobilization on Metal-Organic Framework (MOF): Effects on Thermostability and Function." Protein & Peptide Letters 26, no. 9 (September 16, 2019): 636–47. http://dx.doi.org/10.2174/0929866526666190430120046.

Full text

Abstract:

MOFs are porous materials with adjustable porosity ensuing a tenable surface area and stability. MOFs consist of metal containing joint where organic ligands are linked with coordination bonding rendering a unique architecture favouring the diverse applications in attachment of enzymes, Chemical catalysis, Gases storage and separation, biomedicals. In the past few years immobilization of soluble enzymes on/in MOF has been the topic of interest for scientists working in diverse field. The activity of enzyme, reusability, storage, chemical and thermal stability, affinity with substrate can be greatly improved by immobilizing of enzyme on MOFs. Along with improvement in enzymes properties, the high loading of enzyme is also observed while using MOFs as immobilization support. In this review a detail study of immobilization on/in Metalorganic Frameworks (MOFs) have been described. Furthermore, strategies for the enzyme immobilization on MOFs and resulting in improved catalytic performance of immobilized enzymes have been reported.

APA, Harvard, Vancouver, ISO, and other styles

15

Zarzycki, Jan, Onur Erbilgin, and Cheryl A. Kerfeld. "Bioinformatic Characterization of Glycyl Radical Enzyme-Associated Bacterial Microcompartments." Applied and Environmental Microbiology 81, no. 24 (September 25, 2015): 8315–29. http://dx.doi.org/10.1128/aem.02587-15.

Full text

Abstract:

ABSTRACTBacterial microcompartments (BMCs) are proteinaceous organelles encapsulating enzymes that catalyze sequential reactions of metabolic pathways. BMCs are phylogenetically widespread; however, only a few BMCs have been experimentally characterized. Among them are the carboxysomes and the propanediol- and ethanolamine-utilizing microcompartments, which play diverse metabolic and ecological roles. The substrate of a BMC is defined by its signature enzyme. In catabolic BMCs, this enzyme typically generates an aldehyde. Recently, it was shown that the most prevalent signature enzymes encoded by BMC loci are glycyl radical enzymes, yet little is known about the function of these BMCs. Here we characterize the glycyl radical enzyme-associated microcompartment (GRM) loci using a combination of bioinformatic analyses and active-site and structural modeling to show that the GRMs comprise five subtypes. We predict distinct functions for the GRMs, including the degradation of choline, propanediol, and fuculose phosphate. This is the first family of BMCs for which identification of the signature enzyme is insufficient for predicting function. The distinct GRM functions are also reflected in differences in shell composition and apparently different assembly pathways. The GRMs are the counterparts of the vitamin B12-dependent propanediol- and ethanolamine-utilizing BMCs, which are frequently associated with virulence. This study provides a comprehensive foundation for experimental investigations of the diverse roles of GRMs. Understanding this plasticity of function within a single BMC family, including characterization of differences in permeability and assembly, can inform approaches to BMC bioengineering and the design of therapeutics.

APA, Harvard, Vancouver, ISO, and other styles

16

Fiehn, Oliver, Dinesh K. Barupal, and Tobias Kind. "Extending Biochemical Databases by Metabolomic Surveys." Journal of Biological Chemistry 286, no. 27 (May 12, 2011): 23637–43. http://dx.doi.org/10.1074/jbc.r110.173617.

Full text

Abstract:

Metabolomics can map the large metabolic diversity in species, organs, or cell types. In addition to gains in enzyme specificity, many enzymes have retained substrate and reaction promiscuity. Enzyme promiscuity and the large number of enzymes with unknown enzyme function may explain the presence of a plethora of unidentified compounds in metabolomic studies. Cataloguing the identity and differential abundance of all detectable metabolites in metabolomic repositories may detail which compounds and pathways contribute to vital biological functions. The current status in metabolic databases is reviewed concomitant with tools to map and visualize the metabolome.

APA, Harvard, Vancouver, ISO, and other styles

17

IKEDA, Tokuji. "Enzyme-modified electrodes with bioelectrocatalytic function." Bunseki kagaku 44, no. 5 (1995): 333–54. http://dx.doi.org/10.2116/bunsekikagaku.44.333.

Full text

APA, Harvard, Vancouver, ISO, and other styles

18

Dalby, Paul A. "Optimising enzyme function by directed evolution." Current Opinion in Structural Biology 13, no. 4 (August 2003): 500–505. http://dx.doi.org/10.1016/s0959-440x(03)00101-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Brokaw, C. J. "Mechanical components of motor enzyme function." Biophysical Journal 73, no. 2 (August 1997): 938–51. http://dx.doi.org/10.1016/s0006-3495(97)78126-8.

Full text

APA, Harvard, Vancouver, ISO, and other styles

20

Rost, Burkhard. "Enzyme Function Less Conserved than Anticipated." Journal of Molecular Biology 318, no. 2 (April 2002): 595–608. http://dx.doi.org/10.1016/s0022-2836(02)00016-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Sakiyama, Fumio. "Modification of enzyme structure and function." Kobunshi 35, no. 10 (1986): 950–53. http://dx.doi.org/10.1295/kobunshi.35.950.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Sharma, Krishna Kant, and Ramesh Chander Kuhad. "Laccase: enzyme revisited and function redefined." Indian Journal of Microbiology 48, no. 3 (June 18, 2008): 309–16. http://dx.doi.org/10.1007/s12088-008-0028-z.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Yoshikuni, Yasuo, Thomas E. Ferrin, and Jay D. Keasling. "Designed divergent evolution of enzyme function." Nature 440, no. 7087 (April 1, 2006): 1078–82. http://dx.doi.org/10.1038/nature04607.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Taivonen, Hannu J., Nevine Makari, and John D. Catravas. "Monitoring of Pulmonary Endothelial Enzyme Function." Anesthesiology 68, no. 1 (January 1, 1988): 44–52. http://dx.doi.org/10.1097/00000542-198801000-00008.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Baly, Deborah L. "Manganese in Metabolism and Enzyme Function." Journal of Nutrition 119, no. 2 (February 1, 1989): 327. http://dx.doi.org/10.1093/jn/119.2.327.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Thiele, Alexandra, Gabriele I. Stangl, and Mike Schutkowski. "Deciphering Enzyme Function Using Peptide Arrays." Molecular Biotechnology 49, no. 3 (May 22, 2011): 283–305. http://dx.doi.org/10.1007/s12033-011-9402-x.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Memon, Safyan Aman, Kinaan Aamir Khan, and Hammad Naveed. "Enzyme Function Prediction using Deep Learning." Biophysical Journal 118, no. 3 (February 2020): 533a. http://dx.doi.org/10.1016/j.bpj.2019.11.2926.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Minshull, Jeremy, Jon E. Ness, Claes Gustafsson, and Sridhar Govindarajan. "Predicting enzyme function from protein sequence." Current Opinion in Chemical Biology 9, no. 2 (April 2005): 202–9. http://dx.doi.org/10.1016/j.cbpa.2005.02.003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

29

Dean, Antony M., Daniel E. Dykhuizen, and Daniel L. Hartl. "Fitness as a function of β-galactosidase activity inEscherichia coli." Genetical Research 48, no. 1 (August 1986): 1–8. http://dx.doi.org/10.1017/s0016672300024587.

Full text

Abstract:

SummaryChemostat cultures in which the limiting nutrient was lactose have been used to study the relative growth rate ofEscherichia coliin relation to the enzyme activity of β-galactosidase. A novel genetic procedure was employed in order to obtain amino acid substitutions within thelacZ-encoded β-galactosidase that result in differences in enzyme activity too small to be detected by ordinary mutant screens. The cryptic substitutions were obtained as spontaneous revertants of nonsense mutations within thelacZgene, and the enzymes differing from wild type were identified by means of polyacrylamide gel electrophoresis or thermal denaturation studies. The relation between enzyme activity and growth rate of these and other mutants supports a model of intermediary metabolism in which the flux of substrate through a metabolic pathway is represented by a concave function of the activity of any enzyme in the pathway. The consequence is that small differences in enzyme activity from wild type result in even smaller changes in fitness.

APA, Harvard, Vancouver, ISO, and other styles

30

Busk, Peter Kamp, and Lene Lange. "Function-Based Classification of Carbohydrate-Active Enzymes by Recognition of Short, Conserved Peptide Motifs." Applied and Environmental Microbiology 79, no. 11 (March 22, 2013): 3380–91. http://dx.doi.org/10.1128/aem.03803-12.

Full text

Abstract:

ABSTRACTFunctional prediction of carbohydrate-active enzymes is difficult due to low sequence identity. However, similar enzymes often share a few short motifs, e.g., around the active site, even when the overall sequences are very different. To exploit this notion for functional prediction of carbohydrate-active enzymes, we developed a simple algorithm, peptide pattern recognition (PPR), that can divide proteins into groups of sequences that share a set of short conserved sequences. When this method was used on 118 glycoside hydrolase 5 proteins with 9% average pairwise identity and representing four characterized enzymatic functions, 97% of the proteins were sorted into groups correlating with their enzymatic activity. Furthermore, we analyzed 8,138 glycoside hydrolase 13 proteins including 204 experimentally characterized enzymes with 28 different functions. There was a 91% correlation between group and enzyme activity. These results indicate that the function of carbohydrate-active enzymes can be predicted with high precision by finding short, conserved motifs in their sequences. The glycoside hydrolase 61 family is important for fungal biomass conversion, but only a few proteins of this family have been functionally characterized. Interestingly, PPR divided 743 glycoside hydrolase 61 proteins into 16 subfamilies useful for targeted investigation of the function of these proteins and pinpointed three conserved motifs with putative importance for enzyme activity. Furthermore, the conserved sequences were useful for cloning of new, subfamily-specific glycoside hydrolase 61 proteins from 14 fungi. In conclusion, identification of conserved sequence motifs is a new approach to sequence analysis that can predict carbohydrate-active enzyme functions with high precision.

APA, Harvard, Vancouver, ISO, and other styles

31

Tan, Jiu-Xin, Hao Lv, Fang Wang, Fu-Ying Dao, Wei Chen, and Hui Ding. "A Survey for Predicting Enzyme Family Classes Using Machine Learning Methods." Current Drug Targets 20, no. 5 (March 5, 2019): 540–50. http://dx.doi.org/10.2174/1389450119666181002143355.

Full text

Abstract:

Enzymes are proteins that act as biological catalysts to speed up cellular biochemical processes. According to their main Enzyme Commission (EC) numbers, enzymes are divided into six categories: EC-1: oxidoreductase; EC-2: transferase; EC-3: hydrolase; EC-4: lyase; EC-5: isomerase and EC-6: synthetase. Different enzymes have different biological functions and acting objects. Therefore, knowing which family an enzyme belongs to can help infer its catalytic mechanism and provide information about the relevant biological function. With the large amount of protein sequences influxing into databanks in the post-genomics age, the annotation of the family for an enzyme is very important. Since the experimental methods are cost ineffective, bioinformatics tool will be a great help for accurately classifying the family of the enzymes. In this review, we summarized the application of machine learning methods in the prediction of enzyme family from different aspects. We hope that this review will provide insights and inspirations for the researches on enzyme family classification.

APA, Harvard, Vancouver, ISO, and other styles

32

Cieśla, Joanna. "Metabolic enzymes that bind RNA: yet another level of cellular regulatory network?" Acta Biochimica Polonica 53, no. 1 (January 12, 2006): 11–32. http://dx.doi.org/10.18388/abp.2006_3360.

Full text

Abstract:

Several enzymes that were originally characterized to have one defined function in intermediatory metabolism are now shown to participate in a number of other cellular processes. Multifunctional proteins may be crucial for building of the highly complex networks that maintain the function and structure in the eukaryotic cell possessing a relatively low number of protein-encoding genes. One facet of this phenomenon, on which I will focus in this review, is the interaction of metabolic enzymes with RNA. The list of such enzymes known to be associated with RNA is constantly expanding, but the most intriguing question remains unanswered: are the metabolic enzyme-RNA interactions relevant in the regulation of cell metabolism? It has been proposed that metabolic RNA-binding enzymes participate in general regulatory circuits linking a metabolic function to a regulatory mechanism, similar to the situation of the metabolic enzyme aconitase, which also functions as iron-responsive RNA-binding regulatory element. However, some authors have cautioned that some of such enzymes may merely represent "molecular fossils" of the transition from an RNA to a protein world and that the RNA-binding properties may not have a functional significance. Here I will describe enzymes that have been shown to interact with RNA (in several cases a newly discovered RNA-binding protein has been identified as a well-known metabolic enzyme) and particularly point out those whose ability to interact with RNA seems to have a proven physiological significance. I will also try to depict the molecular switch between an enzyme's metabolic and regulatory functions in cases where such a mechanism has been elucidated. For most of these enzymes relations between their enzymatic functions and RNA metabolism are unclear or seem not to exist. All these enzymes are ancient, as judged by their wide distribution, and participate in fundamental biochemical pathways.

APA, Harvard, Vancouver, ISO, and other styles

33

Arnold, Frances H. "Enzymes by Evolution: Bringing New Chemistry to Life." Molecular Frontiers Journal 02, no. 01 (January 2018): 9–18. http://dx.doi.org/10.1142/s2529732518400023.

Full text

Abstract:

Not satisfied with nature’s vast enzyme repertoire, we want to create new ones and expand the space of genetically encoded enzyme functions. We use the most powerful biological design process, evolution, to optimize existing enzymes and invent new ones, thereby circumventing our profound ignorance of how sequence encodes function. Mimicking nature’s evolutionary tricks and using a little chemical intuition, we can generate whole new enzyme families that catalyze important reactions, including ones not known in biology. These new capabilities increase the scope of molecules and materials we can build using biology.

APA, Harvard, Vancouver, ISO, and other styles

34

Maria-Solano, Miguel A., Eila Serrano-Hervás, Adrian Romero-Rivera, Javier Iglesias-Fernández, and Sílvia Osuna. "Role of conformational dynamics in the evolution of novel enzyme function." Chemical Communications 54, no. 50 (2018): 6622–34. http://dx.doi.org/10.1039/c8cc02426j.

Full text

Abstract:

Enzymes exist as a dynamic ensemble of conformations, each potentially playing a key role in substrate binding, the chemical transformation, or product release. We discuss recent advances in the evaluation of the enzyme conformational dynamics and its evolution towards new functions or substrate preferences.

APA, Harvard, Vancouver, ISO, and other styles

35

Ptak, Christopher, Chantelle Gwozd, J. Torin Huzil, Todd J. Gwozd, Grace Garen, and Michael J. Ellison. "Creation of a Pluripotent Ubiquitin-Conjugating Enzyme." Molecular and Cellular Biology 21, no. 19 (October 1, 2001): 6537–48. http://dx.doi.org/10.1128/mcb.21.19.6537-6548.2001.

Full text

Abstract:

ABSTRACT We describe the creation of a pluripotent ubiquitin-conjugating enzyme (E2) generated through a single amino acid substitution within the catalytic domain of RAD6 (UBC2). This RAD6 derivative carries out the stress-related function of UBC4 and the cell cycle function of CDC34 while maintaining its own DNA repair function. Furthermore, it carries out CDC34's function in the absence of the CDC34 carboxy-terminal extension. By using sequence and structural comparisons, the residues that define the unique functions of these three E2s were found on the E2 catalytic face partitioned to either side by a conserved divide. One of these patches corresponds to a binding site for both HECT and RING domain proteins, suggesting that a single substitution in the catalytic domain of RAD6 confers upon it the ability to interact with multiple ubiquitin protein ligases (E3s). Other amino acid substitutions made within the catalytic domain of RAD6 either caused loss of its DNA repair function or modified its ability to carry out multiple E2 functions. These observations suggest that while HECT and RING domain binding may generally be localized to a specific patch on the E2 surface, other regions of the functional E2 face also play a role in specificity. Finally, these data also indicate that RAD6 uses a different functional region than either UBC4 or CDC34, allowing it to acquire the functions of these E2s while maintaining its own. The pluripotent RAD6 derivative, coupled with sequence, structural, and phylogenetic data, suggests that E2s have diverged from a common multifunctional progenitor.

APA, Harvard, Vancouver, ISO, and other styles

36

Holliday, Michael Joseph, Carlo Camilloni, Geoffrey Stuart Armstrong, Michele Vendruscolo, and Elan Zohar Eisenmesser. "Networks of Dynamic Allostery Regulate Enzyme Function." Structure 25, no. 2 (February 2017): 276–86. http://dx.doi.org/10.1016/j.str.2016.12.003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Hatzimanikatis, Vassily, Chunhui Li, Justin A. Ionita, and Linda J. Broadbelt. "Metabolic networks: enzyme function and metabolite structure." Current Opinion in Structural Biology 14, no. 3 (June 2004): 300–306. http://dx.doi.org/10.1016/j.sbi.2004.04.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Frankish, Helen. "Researchers uncover function of key Alzheimer's enzyme." Lancet Neurology 5, no. 11 (November 2006): 904. http://dx.doi.org/10.1016/s1474-4422(06)70589-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

39

Thornton, Janet. "THE EVOLUTION OF ENZYME STRUCTURE AND FUNCTION." Biochemical Society Transactions 28, no. 3 (June 1, 2000): A53. http://dx.doi.org/10.1042/bst028a053.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Mason, Nancy A. "Angiotensin-Converting Enzyme Inhibitors and Renal Function." DICP 24, no. 5 (May 1990): 496–505. http://dx.doi.org/10.1177/106002809002400511.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Keller, F., C. Emde, and A. Schwarz. "Exponential function for calculating saturable enzyme kinetics." Clinical Chemistry 34, no. 12 (December 1, 1988): 2486–89. http://dx.doi.org/10.1093/clinchem/34.12.2486.

Full text

Abstract:

Abstract Enzyme kinetics are usually described by the Michaelis-Menten equation, where the time-dependent decrease of substrate (-dS/dt) is a hyperbolic function of maximal velocity (Vmax), Michaelis constant (Km), and amount of substrate (S). Because the Michaelis-Menten function in its most general meaning requires an assumption of steady-state, it is less curvilinear than true enzyme kinetics. A saturation-type exponential function is more curvilinear than the hyperbolic function and more closely approximates enzyme kinetics: -dS/dt = Vmax [1 - exp(-S/Km)]. The mathematical representation of enzyme kinetics can be further improved by introducing a deceleration term (Vdec), to make the assumption of a steady state unnecessary. For the action of chymotrypsin on N-acetyltyrosylethylester, the Michaelis-Menten equation yields the following: Vmax = 3.74 mumol/min and Km = 833 mumol. According to decelerated enzyme kinetics, the values Vmax = 4.80 mumol/min, Vdec = 0.0118 mumol/min, and the association constant (Ka) = 0.00111/mumol are more nearly accurate for this reaction (where 1/Ka = 901 mumol approximately Km).

APA, Harvard, Vancouver, ISO, and other styles

42

LEE, JINAH. "Function of Deubiquitinating Enzyme USP1 in Adipogenesis." Diabetes 67, Supplement 1 (May 2018): 284—LB. http://dx.doi.org/10.2337/db18-284-lb.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Kuriki, Takashi, Han-Ping Guan, and Jack Preiss. "Structure and Function of Starch Branching Enzyme." Journal of the agricultural chemical society of Japan 68, no. 11 (1994): 1581–84. http://dx.doi.org/10.1271/nogeikagaku1924.68.1581.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Brokaw, Charles J. "Weakly-coupled models for motor enzyme function." Journal of Muscle Research and Cell Motility 16, no. 3 (June 1995): 197–211. http://dx.doi.org/10.1007/bf00121129.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Kim, Jungbae, and Jonathan S. Dordick. "Pressure affects enzyme function in organic media." Biotechnology and Bioengineering 42, no. 6 (September 5, 1993): 772–76. http://dx.doi.org/10.1002/bit.260420613.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

White, Robert H. "The Twists and Turns of Enzyme Function." Journal of Bacteriology 192, no. 8 (February 12, 2010): 2023–25. http://dx.doi.org/10.1128/jb.00087-10.

Full text

APA, Harvard, Vancouver, ISO, and other styles

47

Astikainen, Katja, Liisa Holm, Esa Pitkänen, Sandor Szedmak, and Juho Rousu. "Towards structured output prediction of enzyme function." BMC Proceedings 2, Suppl 4 (2008): S2. http://dx.doi.org/10.1186/1753-6561-2-s4-s2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

von Grotthuss, M., D. Plewczynski, G. Vriend, and L. Rychlewski. "3D-Fun: predicting enzyme function from structure." Nucleic Acids Research 36, Web Server (May 19, 2008): W303—W307. http://dx.doi.org/10.1093/nar/gkn308.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Gifford, Stacey M., and Pablo Meyer. "Enzyme function is regulated by its localization." Computational Biology and Chemistry 59 (December 2015): 113–22. http://dx.doi.org/10.1016/j.compbiolchem.2015.08.004.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Duckworth, Benjamin P., and Courtney C. Aldrich. "Assigning Enzyme Function from the Metabolic Milieu." Chemistry & Biology 17, no. 4 (April 2010): 313–14. http://dx.doi.org/10.1016/j.chembiol.2010.04.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Journal articles on the topic 'Enzyme function'

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles