Exploring the Dynamics of Enzyme Activity: Environmental and Biological Influences
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Abstract
The work presents the classification of enzymes and factors that are affecting enzymatic reactions in the living systems. Factors such as temperature, pH, enzyme concentration, substrate concentration, factors of inhibition, factors of activation, and incubation time are important in influencing enzyme reactions, which are responsible for controlling components in living systems. The majority of enzymes are three-dimensional molecules with complex molecular networks and sensitive to various environmental factors.
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References
MurpHy JM, et al. (2014). "A robust methodology to subclassifypseudokinases based on their nucleotide-binding properties". Biochemical Journal. 457 (2): 323–334.
Schomburg I, Chang A, Placzek S, Söhngen C, Rother M, Lang M, Munaretto C, Ulas S, Stelzer M, Grote A, Scheer M, Schomburg D (January 2013). "BRENDA in 2013: integrated reactions, kinetic data, enzyme function data, improved disease classification: new options and contents in BRENDA". Nucleic Acids Research. 41
Callahan BP, Miller BG (December 2007). "OMP decarboxylase—An enigma persists". Bioorganic Chemistry. 35 (6): 465–9.
Vasella A, Davies GJ, Böhm M (October 2002). "Glycosidase mechanisms".Current Opinion in Chemical Biology. 6 (5): 619–29.
Boyer R (2002). "Chapter 6: Enzymes I, Reactions, Kinetics, and Inhibition". Concepts in Biochemistry (2nd ed.). New York, Chichester, Weinheim, Brisbane, Singapore, Toronto.: John Wiley & Sons, Inc. pp. 137–8.
Warshel A, Sharma PK, Kato M, Xiang Y, Liu H, Olsson MH (August 2006). "Electrostatic basis for enzyme catalysis". Chemical Reviews. 106 (8): 3210–35.
Cox MM, Nelson DL (2013). "Chapter 6.2: How enzymes work". Lehninger Principles of Biochemistry (6th ed.). New York, N.Y.: W.H. Freeman. p. 195.
Benkovic SJ, Hammes-Schiffer S (August 2003). "A perspective on enzyme catalysis".Science. 301 (5637): 1196–202.
Villa J, Strajbl M, Glennon TM, Sham YY, Chu ZT, Warshel A (October 2000). "How important are entropic contributions to enzyme catalysis?".Proceedings of the National Academy of Sciences of the United States of America. 97 (22): 11899–904. .
Polgár, L. (7 July 2005). "The catalytic triad of serine peptidases".Cellular and Molecular Life Sciences. 62 (19–20): 2161–2172.
Ramanathan A, Savol A, Burger V, Chennubhotla CS, Agarwal PK (2014). "Protein conformational populations and functionally relevant substates". Acc. Chem. Res. 47(1): 149–56.
Tsai CJ, Del Sol A, Nussinov R (2009). "Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms" (PDF). MolBiosyst. 5(3): 207–16.
Changeux JP, Edelstein SJ (June 2005). "Allosteric mechanisms of signal transduction".Science. 308 (5727): 1424–8.
Voet D, Voet J, Pratt C (2016). Fundamentals of Biochemistry. Hoboken, New Jersey: John Wiley & Sons, Inc. p. 336.
Fisher Z, Hernandez Prada JA, Tu C, Duda D, Yoshioka C, An H, Govindasamy L, Silverman DN, McKenna R (February 2005). "Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II".Biochemistry. 44 (4): 1097–115.
Noree C, Sato BK, Broyer RM, Wilhelm JE (August 2010). "Identification of novel filament-forming proteins in Saccharomyces cerevisiae and DrosopHilamelanogaster".The Journal of Cell Biology. 190 (4): 541–51.
Aughey GN, Liu JL (2015). "Metabolic regulation via enzyme filamentation".Critical Reviews in Biochemistry and Molecular Biology. 51 (4): 282–93.




















