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EDIT: Thanks a lot to @abukaj for pointing out the mistake in my answer (and to @paracetamol for asking such a beautiful question). I am rewriting my answer to incorporate the (hopefully) correct background knowledge this time.
NEW ANSWER: As @paracetamol and @AlanBoyd (in their answer) pointed out the lack of credible support for the claim that infants ...
answered Mar 22 '17 at 11:54
another 'Homo sapien'
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Enzymes alter the rate of a reaction by lowering activation energy; they have no effect on the reaction equilibrium ($\ce{K_{eq}}$). Since $\ce{K_{eq}=\frac{k_f}{k_r}}$ and $\ce{K_{eq}}$ is constant, an increase in forward rate ($\ce{k_f}$) requires a corresponding increase in the reverse rate ($\ce{k_r}$). Intuitively it may help to think that the same ...
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Short answer
The direction of rotation depends on the viewing point of the observer and the reaction catalyzed by the ATP synthase. When synthesizing ATP, and viewed 'from the bottom' (observer faces the intermembrane space looking into the mitochondrial matrix) it rotates clockwise.
Background
ATP synthase is a membrane bound enzyme with two large subunits;...
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Enzymes can catalyze a thermodynamically unfavorable reaction by coupling it with a thermodynamically favorable reaction. Most often, enzymes use ATP hydrolysis reaction (energetically favorable) as a source of energy (in simple terms) to drive the unfavorable reaction forward. One important point to keep in mind here is that enzymes don't drive a reaction ...
answered Jun 26 '17 at 8:58
another 'Homo sapien'
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While it's true that cellulose is full of calories, it's very difficult to get the calories out.
Symbiotic bacteria take ages to digest cellulose, and as a result animals that digest cellulose with specialized symbiotic bacteria have a huge gut to house them in.
It's likely that the reason humans can't digest cellulose is because mammals generally can't. ...
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Can enzymes catalyze thermodynamically unfavourable reactions?
Enzymes don't change the equilibrium of a reaction, but the fact that an equilibrium exists means that the reaction proceeds in both the forward and reverse directions. Before equilibrium is attained, ΔG for the reaction is not 0. Thus, by definition, one direction is thermodynamically ...
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No, not all enzymes (or other proteins for that matter) can be obtained in functional form by recombinant expression with today's methods. As you suspect, problems arise when complex post-translational modifications are necessary to obtain the correct function.
Direct modifications to peptide is one potential problem. Some of these can be resolved by ...
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This terminology is at least as old as September 1944 when Enzymatic Synthesis of Acetyl Phosphate Journal of Biological Chemistry
155, 55-70 was published by Lipmann, which says:
Inorganic phosphate, referred to as Pi, was estimated
colorimetrically
See also the definition of "inorganic phosphate" and "orthophosphate" from this 1943 ...
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What about the ATP synthase? https://en.wikipedia.org/wiki/ATP_synthase it uses proton flow to generate ATP but it can also burn ATP to generate proton flow.
Like other enzymes, the activity of F1FO ATP synthase is reversible.
Large-enough quantities of ATP cause it to create a transmembrane
proton gradient, this is used by fermenting bacteria that do ...
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As @Chris commented, when assayed in vitro with a single substrate (which may not even be the physiological one) most enzymes can catalyse a reaction in either direction. And enzymes such as pyruvate kinase were discovered before the pathways they are constituents of were worked out in full. Furthermore, the ways of naming enzymes only became more ...
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This seems one form of a common question about evolution.
That being: "Trait X would seem to be an advantage, so why can't organisms adapt to X?
That is, why don't we have all traits that are advantageous at all? Why not just digest cellulose, but maybe why not lignin as well? Why shouldn't we photosynthesize our own food? What about sonar as well ...
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The answer given by Sadegh gives a general correct broad view. But one part of the puzzle is missing, which is molecular recognition.
Molecules bind to each other via physical/chemical interaction like forming hydrogen bonds, electrostatic interactions and other mechanisms. The sum of all interaction defines the strength of the binding. If molecules have ...
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Yes, something can be both a hormone and an enzyme. There are a group of hormones known as peptide hormones. These are proteins (such as enzymes) that act as hormones indirectly (and maybe directly too?). A hormone is a chemical secreted by a cell that has some effect on another cell elsewhere in the body. In this case, the chemical just happens to be an ...
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How are diabetes and obesity connected in light of low lipase activity?
Short answer: There's more than one type of diabetes. (And to complicate things, there's also more than one type of lipase. It's unclear from the question which type were mentioned in what you read.)
Diabetes mellitus is usually divided into Type 1 (insulin-deficient) and Type 2 (...
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The mechanism of aconitase classifies it as a lyase, even if (under most physiological conditions), the relative concentrations of substrates results in it catalysing the conversion of citrate to isocitrate. In short, it is not an isomerase because the substrate is released after each step.
As the mechanism of aconitase shows, it catalyses the conversion of ...
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Examples of enzymes working in reverse?
Except three enzymes of Glycolysis (Hexokinase, PFK-I and Pyruvate kinase) all catalyse reversible reactions.
As these enzymes catalyse the backward reactions too they are part of Gluconeogenesis pathway.
(A comparison between the two pathways)
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Until the late 1980's all enzymes* were believed to be proteins, and were often defined as protein catalysts, often in textbooks which are often not perfect representations of science. At that point every macromolecular biological catalyst known was a protein so they thought all macromolecular catalysts were proteins. But the discovery of ribozymes (RNA ...
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It's both simple and complex. The simple answer is Brownian motion. All the particles in the cell do have mobility which is related to their mass. A small particle like a soluble enzyme undergoes random walks through the cytoplasm or nucleoplasm. Thus by having a grand number of a certain molecule you can be sure that at some point it interacts with the ...
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Why don't we have any enzyme to digest cellulose?
Why should we? We don't use it as a source of energy so why bother? Even animals that do "digest" cellulose, like ruminants, only do so because of symbiotic bacteria; it would be a poor system indeed in which every organism utilized the same resource. We occupy enough of the food chain as it is.
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The short answer to this question is given in the Wikipedia article on glycerol kinase:
Adipocytes lack glycerol kinase so they cannot metabolize the glycerol produced during triacyl glycerol degradation. This glycerol is instead shuttled to the liver via the blood where it is: phosphorylated by glycerol kinase to glycerol phosphate and/or converted to ...
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Competitive inhibitor competes for the active site. Therefore it will interfere with the binding of the substrate thereby increasing the apparent KM.
A strictly non-competitive inhibitor does not compete for the active site. It however inhibits the catalysis by reducing the available molecules of active enzyme, E0 (if it is a perfect inhibitor), thereby ...
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You mention nucleases and proteases, but if you turn these processes around and think about the actual nucleic acid or protein synthesis reactions an interesting point emerges:
These synthetic processes involve the production of pyrophosphate — not
orthophosphate — from ATP (etc.).
(In the case of nucleic acid synthesis this should be obvious; in the ...
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Is there a difference in the gene encoding for the protease?
This paper by Wu et al. annotates the SARS-CoV-2 genome and compares its divergence from other coronaviruses, which may help answer your second question.
This annotation includes 16 genes for non-structural protein ("nsp"). Supplemental materials for this paper indicate that all but two of these ...
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Proteins are polymers of amino acids. Each amino acid has a side chain. Many of these side chains contain ionisable groups. The ionization state of these groups is dependent on the pH. A group that is protonated at pH=2 and neutral, for example, may become deprotonated at pH=8 and become negative. See the Henderson-Hasselbalch equation.
Protein structure is ...
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In human cells it takes about 20 s to make a 20,000 dalton enzyme.
Assuming that the cells concerned are already making mRNA for the enzyme, there will be two main factors:
(1) The time taken to synthesize the polypeptide
(2) Any time taken to fold the protein
(If the enzyme is secreted from the cell there will also be the time taken for the protein to ...
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The article referred to in the question is Fromme et al. (2004). I was able to find several proposed mechanisms for the monofunctional uracil-DNA glycosylase but I'll discuss two that seem most relevant in the context of your question.
The first I'll mention was outline by Parikh et al. (2000) who studied recombinant human mitochondrial uracil-DNA ...
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Both parts overlap. Proteins are a chain of linked amino acids. This chain can be grouped into functional units which are called protein domains. Usually all parts of a domain are closely located in the protein and they form functional domains in the 3D structure of the protein. Proteins usually contain more than one domain (these are manifold but for ...
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In my experience 10min at 100°C are sufficient, this is also supported by the paper linked below. Heat inactivation works by denaturing the protein and is therefore final.
Depending on what you want to do with you sample, it might be problematic, as this is probably also denaturated at least to some degree.
You can also chemically inactivate trypsin, ...
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