Questions tagged [enzymes]

Enzymes are macromolecular biological catalysts that alter the rate of a reaction. Use this tag for question regarding enzyme kinetics, classification and action.

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10
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4answers
276 views

What is an example of chemical reaction that can be assisted by both an inorganic catalyst and an enzyme?

I have been researching chemical reactions of inorganic catalysts and enzymes and cannot find a chemical process where an inorganic compound can be replaced by an enzyme (or vice versa) and have the ...
2
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0answers
54 views

How to find the reaction rate in an enzyme reaction?

First time posting questions here, so let me know if I need to edit anything. I need to decide $dC/dt$ and $dP/dt$ when the reaction is like this, where I only know we must have 2 substrates $S$ to ...
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0answers
22 views

Why does allosteric binding produce a sigmoidal curve?

Allosteric binding is where the enzyme can be regulated through having ligands bind onto somewhere that is not the active site. This will then induce a conformational change on the active site, hence ...
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3answers
328 views

Why use Km in catalytic efficiency?

The catalytic efficiency of an enzyme is given by $k_{cat}/k_M$ where $k_{cat}$ is the turnover number, or the number of molecules that can be produced per second per active site of an enzyme. $K_{M}$ ...
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1answer
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Do phosphoryl thiocholines, their uncharged analogs, and other organophosphates, interact differently with Acetylcholinesterase?

As asked in the title, would the various salts -such as hydrochloride or methyl iodide- of V-Agents interact any differently with acetylcholinesterase compared to the neutral compound? For instance, ...
2
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1answer
47 views

Is Km the concentration needed to keep the enzyme running at max speed?

$K_m$ is the Michaelis constant, which is the concentration of substrate needed to achieve a rate of $\frac{V_{max}}{2}$. $V_{max}$ is the maximum number of molecules that can be reacted per second. ...
5
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1answer
86 views

How do enzymes affect a reaction's equilibrium?

I am not sure to understand something I read in a educational journal (1) Introduction Lets consider the following reversible enzyme-catalysed reversible reaction; $$E + S \leftrightharpoons ES \...
2
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0answers
30 views

Differences in AChE inhibition kinetics between paraoxon and methyl paraoxon

According to literature, dimethyl paraoxon has a reaction rate constant for the aging (spontaneous dealkylation) of acetylcholinesterase of $\pu{0.186 h-1}$, a spontaneous reactivation rate constant ...
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22 views

Differences in AChE inhibition kinetics between VX and VR

According to the referenced paper, VR has an AChE inhibition reaction rate constant almost 4 times that of VX. Interestingly, its reaction rate constant for aging of the enzyme is less than that of VX,...
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13 views

Structure-Activity Relationship of Chlormephos and Parathion

According to the book "The Chemistry of Organophosphorus Pesticides", the insecticide Chlormephos (S-(chloromethyl) O,O-diethyl phosphorodithioate) has an oral LD50 in rats of 7 mg/k. ...
2
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0answers
29 views

How can DI water inhibit peroxidase activity?

I'm troubleshooting an IHC staining issue, and according to Thermo-Fischer's website, "Deionized water can sometimes contain peroxidase inhibitors that can significantly impair enzyme activity.&...
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Why is Chlormephos highly toxic despite requiring metabolic activation?

According to the book "The Chemistry of Organophosphorus Pesticides", the insecticide Chlormephos (S-(chloromethyl) O,O-diethyl phosphorodithioate) has an oral LD50 in rats of 7 mg/kg. For ...
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1answer
60 views

Does the mechanism of AChE inhibition by Isoparathion depend on chirality?

It is known that the inhibition of acetylcholinesterase by isomalathion can proceed either with diethyl succinate as the leaving group or thiomethyl, depending on the specific stereoisomer of ...
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1answer
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Could shear force from blending denature alpha amylase / glucoamylase enzymes?

I am trying to break down the starches in a certain variety of oats in the most efficient way possible. I have to break the whole oats down after cooking, so they are finer particles for the amylases ...
4
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1answer
113 views

Why are isomers of parathion less active acetylcholinesterase inhibitors than paraoxon?

Parathion itself has been found to be a very weak inhibitor of acetylcholinesterase. It normally requires metabolic activation and the conversion into paraoxon in the body to actually start exhibiting ...
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41 views

What is the chemical reaction behind ginger milk curd?

Pouring hot milk into ginger juice solidifies the milk. All I know is that ginger juice contains Zingibain that could break down milk proteins into smaller polypeptides. I'm confused as though why is ...
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0answers
23 views

How do structural differences between neostigmine and TL-599 contribute to differences in toxicity?

Stevens and Beutel studied the activity of several carbamate anticholinesterases. Among other things, they found that the (4-trimethylammonio)phenyl dimethylcarbamate iodide (The para-analog of ...
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Why are S-thiocarbamates less toxic than carbamates?

According to Haley and Rhodes, neostigmine bromide (alternatively known as Prostigmine) has an LD50 in mice of around 0.165 mg/kg by IV injection. Pubchem claims that this is also the LD50 for ...
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50 views

Can bis-quaternary aromatic compounds act directly on acetylcholine receptors?

The book Cholinesterases and Anticholinesterase Agents gives examples of bis-quaternary aromatic compounds that are capable of inhibiting acetylcholinesterase. Page 400 gives examples of some such ...
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23 views

Reaction rate constants for the inhibition of cholinesterases by various carbamates

Darvesh et al. [1] have conducted a study on the anticholinesterase activity of various carbamates derived from phenothiazine. The authors measured the inhibition rate constants of rivastigmine for ...
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2answers
65 views

PLP-Dependent Cyclization and Decarboxylation

I am looking at Compound A (see below) and am trying to figure out a decarboxylation mechanism that results in Compound B (see below). I have come up with an internal mechanism that might work that I ...
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1answer
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Does migraine medicine Topiramate work by supplanting Pyridoxal phosphate in enzymes?

I have seen it said that the precise mechanism of action of migraine medicine Topiramate is not known. But I certainly see a resemblance between that molecule and PLP (Pyridoxal phosphate, the ...
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0answers
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Does cellulase catalyze the hydrolysis (or break down) of soluble starch?

I’m attempting to perform an Iodometric redox titration to evaluate the vitamin c concentration in a particular solution. These solution have dissolved within them up to 2% cellulase enzyme. In an ...
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0answers
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Solving for Concentration Using pseudo-First Order Kinetics

The following graphs represent a pseudo-first order bi-molecular reversible reaction with the formula $\ce{A + B <=> C}$: The reaction product has an extinction coefficient of $\pu{50000 M-1 cm-...
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Does HI-6 form a covalent adduct with acetylcholinesterase?

According to sources provided below, the oxime HI-6, or Asoxime Dichloride, as it is also called, besides being a reactivator of acetylcholinesterase that has been inhibited by organophosphorus ...
2
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1answer
69 views

How to predict amine donor in biochemical reactions (whether glutamine or aspartate)?

In biochemical reactions amine $(\ce{-NH2})$ transfer is done in multiple pathways (e.g. urea cycle, purine biosynthesis etc.). In many of the situations glutamine donates amine group (e.g. xanthosine ...
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2answers
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What is the mechanism of AChE inhibition by Onchidal?

A naturally-occuring neurotoxin, called Onchidal, produced by a species of sea slug acts as an irreversible inhibitor of acetylcholinesterase. The structure of Onchidal is presented below: How and ...
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Hydrolysis of phosphoryl-oximes

When acetylcholinesterase that has been inhibited by an organophosphorus compound is reactivated by an oxime, a phosphoryl-oxime is formed, which is then somehow hydrolyzed in the blood. One study ...
3
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1answer
65 views

Can aged acetylcholinesterase be reactivated?

it is a well-known fact that certain phosphorus compounds can inhibit the enzyme acetylcholinesterase, and that the treatment of poisoning with such compounds is administration of atropine and some ...
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Interaction of trifluoroacetates with acetylcholinesterase

There exists a substance called TMTFA, or 3-(N,N,N-Trimethylammonio)-2,2,2-trifluoroacetophenone. It is known for being able to inhibit acetylcholinesterase at femtomolar concentrations. The TMTFA-...
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Why are carbamates capable of inhibiting acetylcholinesterase?

Certain carbamate compounds, such as the insecticide carbaryl or the Edgewood carbamates such as EA-3990, can inhibit the enzyme acetylcholinesterase. Unlike organophosphorus compounds, however, they ...
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How much glucose oxidase is usually deposited on a glucometer strip?

The concentration of serum glucose is on average roughly around 5 mmol/L and let's say a typical blood droplet applied to a glucometer is 1μL. We are therefore depositing 5 nmol of glucose on the test ...
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4answers
435 views

Why do so many biochemical reactions require enzymes?

Studying biochemistry as part of the Great Courses, I am struck that all 10 steps in glycolysis require an enzyme. I’d have thought that evolution would have selected for a “simpler” pathway with ...
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Collagen digestion

As far as I know, pepsin is used very often in collagen solutions extraction. Since it only cleaves the telopeptides and leaves the triple helix chains of the collagen intact. I was wondering if there ...
5
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1answer
90 views

What is a secondary shell in an enzyme?

I've searched the internet for a definition of what the different shells in enzymes/proteins are and haven't found a good answer. This Nature article, which is about an enzyme that catalyzes Kemp ...
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2answers
304 views

AChE Aging time of organophosphorus compounds containing hydroxyl groups

Organophosphorus compounds are known to inhibit the enzyme acetylcholinesterase (AChE). This occurs when the OPC phosphorylates the serine-203 residue of the enzyme. If the enzyme is not reactivated ...
7
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1answer
89 views

How can subtilisin still function without its catalytic triad?

I read chapter 9 in the book Biochemistry (5th edition), by Berg, Tymoczko, and Stryer (provided in the NCBI site here). It describes the mechanism of action of the chymotrypsin enzyme. The catalysis ...
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0answers
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Given the pH optimum of Angiotensin 1, how do I determine its charge?

I'm given the following information I'm then asked to determine the charge of the substrate Angiotensin 1 at the pH-optimum. I have found the pH-optimum to be 6.9. How do I go about answering this ...
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Is there a software that can predict the shape of a custom protein, given its amino acid sequence?

I know that the internet is full of enzyme and protein simulators which can show active site and 3D structure (like bioblender), but the problem with these programs is that they use predefined ...
6
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3answers
298 views

Representation of bromelain molecule in two dimensional diagram [closed]

If I'm not wrong, I learned in 2011 introduction to neuropsychology course that all enzymes are proteins. As far as I know, any protein, not even the smallest of the TAL group (which I understand to ...
2
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1answer
439 views

What is the definition of a “Simple enzyme” exactly? Is it an enzyme that does not require a co-factor?

I'm having a hard time making a distinction between simple and complex enzymes. the definitions I've found so far all say this: Simple enzymes are enzymes that are only made out of protein, and ...
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0answers
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Convert lactose in milk to Galactooligosaccharides [closed]

There are few articles describing the conversion of lactose to GOS on Wiley Online Library with different enzymes. Yet none of them really talks about what % of the lactose in milk can be converted to ...
4
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2answers
73 views

Enzyme Kinetics

How come enzymes with a lower $K_\mathrm{m}$ are more easily saturated with substrate than an enzyme with higher $K_\mathrm{m}?$ Is it because enzymes with higher $K_\mathrm{m}$ are able to bind ...
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2answers
205 views

Bleaching of chlorophyll stains using hydrogen peroxide

I have been doing some experiments concerning bleaching of chlorophyll stains from cotton clothing. Currently I have found that $\ce{H2O2}$ is fairly effective, but still leaves visible stains. Would ...
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1answer
35 views

Solvents and Enzymes

I was reading recently about environmental remediation being done, using an esterase to break down / neutralize cocaine that had contaminated waterways in Europe. Are there similar enzymes that can be ...
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1answer
630 views

Synthases vs Lyases - nomenclature

Lyases are a class of enzymes that break down (lyase: ly- = lysis, -ase = enzyme) bonds like $\ce{C-C, C-S}$ and so on (except hydrolysis), and can eliminate molecules like $\ce{H2O}$ or $\ce{CO2}$. ...
2
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1answer
73 views

Michaelis menten constant motivation behind 1/2?

So the michaelis constant is defined as the substrate concentration at half maximal „reaction-speed“. I was wondering why 1/2 ? I guess for higher values you need more substrate, which could be a ...
6
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1answer
60 views

Where to find compounds IC50 on an enzyme?

I am looking for half maximal inhibitory concentration (IC50) values on a enzyme. I already searched through ChemBL, PubChem and BindingDB. The three seem to give consistent results. However, ...
0
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1answer
65 views

Inactivation of enzyme: Why inactivation constants do not follow the Arrhenius equation? [closed]

The Arrhenius equation may not account for the temperature effect on thermal inactivation rate constants. Why can the thermal inactivation kinetics not be expected to follow Arrhenius? The reason that ...
1
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1answer
55 views

How to calculate the kinetic order of an enzymatic reaction?

This question is concerning the metabolism of ethanol by an alcohol dehydrogenase enzyme. Usually people metabolize alcohol equivalent to "one beer per hour". One beer is said to contain 33cL. The ...