Alcantara, Joshua G.

17/03/2022

BSN 1-YB-19

1. To which class does each enzyme belong? Explain your answers.

a.) pyruvate decarboxylase

Pyruvate decarboxylase has the EC number 4.1.1.1. It decarboxylates pyruvate and is

classed as a lyases enzyme. It also catalyzes the conversion of pyruvic acid to acetaldehyde through

decarboxylation. Pyruvate decarboxylase is an enzyme that removes the carboxyl group from

pyruvate. Co2 is a member of the lyases family of enzymes that catalyze the dissociation of

chemical bonds. To put it another way, decarboxylation converts pyruvate to acetaldehyde. Then,

through a process catalyzed by alcohol dehydrogenase, NAD+ is replenished when acetaldehyde

is converted to ethanol. Pyruvate decarboxylation takes place in the mitochondrial matrix. The

citric acid cycle will also pass through the acetyl CoA formed by the pyruvate decarboxylation

mechanism in the mitochondrial matrix.

b.) alanine aminotransferase

A group of enzymes known as alanine aminotransferase catalyzes the interconversion of

amino acids and oxoacids. ALAT or ALT is another name for it. Its EC number is EC 2.6.1.2. It's

a transaminase enzyme that's mostly located in the liver and kidney. This enzyme is involved in

cellular nitrogen metabolism, amino acid metabolism, and liver gluconeogenesis. The Alanine

aminotransferase catalyzes the reversible transfer of the glutamate amino group to pyruvate, as

well as the substitution of a carbonyl group for the glutamate amino group. For the ALT-catalyzed
process, the cofactor pyridoxal-5'-phosphate, or P5P, which is the active form of vitamin B6, is

required. P5P then attaches covalently but reversibly to an active site lysine, aiding catalysis by

absorbing the amino group from the amino acid and converting it to a carbonyl molecule.

c.) alcohol dehydrogenase

This enzyme belongs to the oxidoreductase family and is a member of it. Alcohol

dehydrogenase, as the name implies, is in charge of initiating the alcohol metabolism process. It

operates by removing an atom of hydrogen from the alcohol. Alcohol dehydrogenase, according

to my research, is our principal defense against alcohol. Oxidoreductase is a protein that catalyzes

the transfer of electrons from one molecule to another. Because it oxidizes alcohol to acetaldehyde

while also reducing a NAD cofactor to NADH, alcohol dehydrogenase belongs to this class. A

Zn2+ atom is coordinated in the active site by Cys-174, Cys-46, and His-67 and serves to place

the alcohol group of ethanol in the active site.

d.) hexokinase

The primary component of the transferase class includes this type of enzyme. Transferase

enzymes catalyze the transfer of functional groups to substrate, such as phosphate, amino or acetyl,

methyl, or alkyl groups, and finally result in the production of a product containing that functional

group, and hexokinase appears to be one of them. Hexokinase is a member of this family because

it catalyzes the phosphorylation of glucose by ATP to create glucose-6-phosphate.

2. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in

order for a productive reaction to occur. Why, then, is some conformational flexibility also

a requirement for catalysis?

In order for a fruitful reaction to occur, the substrate and reactive groups in an enzyme's

active site must be exactly aligned. But why is conformational flexibility also a need for catalysis?

It keeps the protein in its active state folded. Catalysis necessitates conformational flexibility since

it aids in the binding of substrates. It could also get into the transition condition. That is why it is

one of the most fundamental prerequisites for catalysis.

3. Some plants contain compounds that inhibit serine proteases. It has been hypothesized

that these compounds protect the plant from proteolytic enzymes of insects and

microorganisms that would damage the plant. Tofu, or bean curd, possesses these

compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is

this treatment necessary?

Plant defense proteins that inhibit serine proteases are known as serine protease inhibitors.

In plants, it is beneficial in the sense that it is long-lasting and effective in decreasing pests'

nutritional metabolism, which is another method of pest control in crops. It also protects plants

from phytopathogenic bacteria. Its primary purpose is to regulate proteolytic activity, and it has

been demonstrated in plants that it also regulates endogenous proteolytic activities, such as
protease regulation in seeds. It also plays a role in controlling the plant's cell death during

development.

In tofu and bean curd, however, it is less useful. Trypsin inhibitor, a type of protease inhibitor, is

prevalent in various soy products and is frequently eliminated or destroyed along with other

antinutritional components. The serine protease found in these soy products is a curdling enzyme

that creates Saccharomyces bayanus, a curdling yeast that causes the soybean to coagulate. This

enzyme gives tofu a bad flavor and texture, which can affect the nutritional value of the food as

well as the safety of eating tofu or soy protein products. Ingesting trypsin inhibitors can raise the

number of monitor peptides in the gut, slow digestion, and reduce protein absorption. It can also

produce an elevation in the blood level of cholecystokinin, which stimulates pancreatic exocrine

protein secretion.