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17 votes
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What inactivates pepsin in infants?

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 ...
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15 votes
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Examples of enzymes working in reverse?

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, ...
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13 votes

In which direction does ATP synthase rotate?

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 ...
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13 votes
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Can enzymes catalyze thermodynamically unfavorable reactions?

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 ...
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12 votes

Can enzymes catalyze thermodynamically unfavorable reactions?

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 ...
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11 votes
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Can any enzyme be produced?

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-...
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11 votes
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Origin of the biochemical term, Pi (inorganic phosphate)

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 ...
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11 votes

Examples of enzymes working in reverse?

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 ...
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10 votes
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Origin of enzyme names

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 ...
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9 votes
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How do DNA, enzymes, hormones etc. reach their proper cellular locations?

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 ...
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7 votes
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Why is aconitase classified as a lyase?

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 ...
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7 votes

Identifying type of inhibitor from $K_m$ and $V_{max}$

I think it is possible to identify the type of inhibition from (initial) velocity vs substrate-concentration curves, but it is difficult. The usual way this is done is by using a linear transformation ...
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  • 4,638
7 votes

Examples of enzymes working in reverse?

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 ...
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  • 8,754
7 votes

Are all enzymes proteins?

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 ...
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7 votes

How do DNA, enzymes, hormones etc. reach their proper cellular locations?

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 ...
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7 votes
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What is the function of dihydrofolate reductase in humans?

The poster’s assumption that the sole role of dihydrofolate reductase (DHFR) is to convert folic acid to tetrahydrofolate is incorrect. The enzyme is important in at least two metabolic pathways in ...
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6 votes
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Why is glycerol kinase absent from adipocytes but present in the liver?

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 ...
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6 votes
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Identifying type of inhibitor from $K_m$ and $V_{max}$

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 ...
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  • 35k
6 votes

Examples of enzymes working in reverse?

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 ...
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6 votes
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How does aminoacyl-tRNA synthetase recognize different tRNAs?

You give the answer in your question: binding areas that recognize a particular tRNA through unique identity sites at the acceptor stem and/or anticodon loop of the tRNA. The point is that ...
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6 votes

How is the protease inhibited by lopinavir different in SARS-CoV-2 compared to SARS-CoV?

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 ...
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5 votes

What is the mechanism of monofunctional glycosylases?

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 ...
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5 votes
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How long does it take for a cell to synthesize an enzyme?

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 ...
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5 votes

Why does pH have an effect on enzymes?

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 ...
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5 votes
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What stops telomerase?

Telomerases are tightly controlled on all level: Expression, post-translational modifications and by external factors. I think for this the external factors, a protein class called telomeric proteins. ...
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  • 49.2k
5 votes
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What is a catalytic domain of an enzyme?

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 ...
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5 votes

What is the difference between a phosphotransferase, a phosphatase, a phosphorylase and a kinase?

Don't get caught in the linguistic trap of attaching too much significance to the precise meaning of any one piece of scientific jargon. Nomenclature, the system of naming things, utterly sucks in ...
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5 votes

How to inactivate trypsin permanently by boiling?

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 ...
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