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The enzyme initially has a conformation that attracts its substrate. Enzyme surface is flexible and only the correct catalyst can induce interaction leading to catalysis. Conformational changes may then occur as the substrate is bound. After the reaction products will move away from the enzyme and the active site returns to its initial shape.
RuBisCO is important biologically because it catalyzes the primary chemical reaction by which inorganic carbon enters the biosphere.While many autotrophic bacteria and archaea fix carbon via the reductive acetyl CoA pathway, the 3-hydroxypropionate cycle, or the reverse Krebs cycle, these pathways are relatively small contributors to global carbon fixation compared to that catalyzed by RuBisCO.
Hexokinase-I (HK-I) is an enzyme activator because it draws glucose into the glycolysis pathway. Its function is to phosphorylate glucose releasing glucose-6-phosphate (G6P) as the product. HK-I not only signals the activation of glucose into glycolysis but also maintains a low glucose concentration to facilitate glucose diffusion into the cell.
The binding energy of the enzyme-substrate complex cannot be considered as an external energy which is necessary for the substrate activation. The enzyme of high energy content may firstly transfer some specific energetic group X 1 from catalytic site of the enzyme to the final place of the first bound reactant, then another group X 2 from the ...
The breakdown of maltose in Escherichia coli is controlled by gene activation. [3] The genes that code for the enzymes responsible for maltose catabolism can only be transcribed in the presence of an activator. [3] The activator that controls transcription of the maltose enzymes is "off" in the absence of maltose. [3]
In biochemistry, a zymogen (/ ˈ z aɪ m ə dʒ ən,-m oʊ-/ [1] [2]), also called a proenzyme (/ ˌ p r oʊ ˈ ɛ n z aɪ m / [3] [4]), is an inactive precursor of an enzyme.A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme.
Activation-induced cytidine deaminase, also known as AICDA, AID and single-stranded DNA cytosine deaminase, is a 24 kDa enzyme which in humans is encoded by the AICDA gene. [5] It creates mutations in DNA [6] [7] by deamination of cytosine base, which turns it into uracil (which is recognized as a thymine). In other words, it changes a C:G base ...
Ubiquitin-activating enzymes, also known as E1 enzymes, catalyze the first step in the ubiquitination reaction, which (among other things) can target a protein for degradation via a proteasome. This covalent bond of ubiquitin or ubiquitin-like proteins to targeted proteins is a major mechanism for regulating protein function in eukaryotic ...