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22.2: Biosynthesis of Amino Acids - Biology

22.2: Biosynthesis of Amino Acids - Biology


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In humans

Nonessential amino acids: Alanine, Asparagine, Aspartate, Cysteine, Glutamate, Glutamine, Glycine, Proline, Serine, Tyrosine

Essential amino acids: Arginine*, Histidine, Isoleucine, Leucine, Lysine, Methionine*, Phenylalanine*, Threonine, Tryptophan, Valine

Three of the essential amino acids can be made in humans but need significant supplementation. Arginine is depleted in processing through the urea cycle. When cysteine is low, methionine is used to replace it so its levels fall. If tyrosine is low, phenylalanine is used to replace it.

Glycolytic Intermediates

A. From Glucose-6-Phosphate: His

His

"The enzyme is involved in histidine biosynthesis, as well as purine nucleotide biosynthesis. The enzymes from archaea and bacteria are heterodimeric. A glutaminase component (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 25 A tunnel to a cyclase component, which adds it to the imidazole ring, leading to lysis of the molecule and cyclization of one of the products. The glutminase subunit is only active within the dimeric complex. In fungi and plants the two subunits are combined into a single polypeptide" KEgg - https://www.genome.jp/dbget-bin/www_....3.2.10+R04558

B. From 3-phosphoglycerate: Serine, Glycine and Cysteine

jkjkjj

jkjkjkj

D. From Pyruvate: Ala, Val, Leu, Ile

Ala can easily be synthesized from the alpha-keto acid pyruvate by a transamination reaction, so we will focus our attention on the others, the branched chain nonpolar amino acid Val, Leu, and Ile.

TCA Intermediates

E. From alpha-ketogluatarate: Glu, Gln, Pro, Arg

Since amino acid metabolism is so complex, it's important to constantly review past learning. The image below from section 18.2 shows the relationship among Glu, Gln and keto acids.

As is evident from the figure, glutamic acid can be made directly through transamination of alpha-ketoglutarate by an ammonia donor, while glutamine can be made by the action of glutamine synthase on glutatic acid.

Arg is synthesized in the urea cycle as we have seen before. It can be made from alpha-keto glutarate through the following sequential intermediates: N-acetylglutamate, N-acetylglutamate-phosphate, N-acetylglutamate-semialdehyde, N-acetylornithine to N-acetylcitruline. The is deacetylated to and enters the urea cycle.

Proline:

F. From oxalacetate: Asp, Asn, Met, Thr, Lys

OAA to Asp

This is a a simple transamination

Asp to Lys

"Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes l-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilized by most bacteria, some archaea, some fungi, some algae, and plants (28, 29). The AAA pathway synthesizes l-lysine from α-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and α-aminoadipic acid is an intermediate. This pathway is utilized by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea" https://jb.asm.org/content/192/13/3304

Here present just the diaminopimelic acid DAP pathway.

below:

he reaction proceeds via a ping-pong bi-bi mechanism; pyruvate initially binds to the enzyme via a Schiff base to the ε-amino group of the active site Lys161 residue [Laber92]. This is followed by addition of L-aspartate semialdehyde and transimination leading to cyclization and dissociation of HTPA [Blickling97]. The kinetic mechanism was refined using initial velocity and dead-end inhibition studies at both high and low pH, confirming the ping-pong reaction mechanism of the enzyme [Karsten97]. Surprisingly, Lys161 is not absolutely essential for catalysis

real product of this enzyme being 4-hydroxy-2,3,4,5-tetrahydro-L,L-dipicolinic acid, it is still known in most publications as dihydropicolinate synthase (DHDPS).

4-Hydroxy-tetrahydrodipicolinate synthase, historically called dihydrodipicolinate synthase (DHDPS, DapA) is the first enzyme unique to lysine biosynthesis, catalyzing the condensation of pyruvate and (S)-aspartate β-semialdehyde. This is thought to be the rate-limiting step in lysine biosynthesis after aspartate kinase III [Laber92]. The product of the reaction catalyzed by DapA was identified as (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate (HTPA) [Blickling97].

Asp to Thr

dfxcxc

"Threonine synthase (ThrS) catalyzes the final chemical reaction of l-threonine biosynthesis from its precursor, O-phospho-l-homoserine. As the phosphate ion generated in its former half reaction assists its latter reaction, ThrS is recognized as one of the best examples of product-assisted catalysis

https://pubs.acs.org/doi/10.1021/acs...ed%20catalysis.

ThrS processes the most complicated reaction of the PLP enzymes, and all seven types of the intermediate states known for PLP enzymes are formed during its catalytic cycle. As the result, there are many chances of side reactions taking place

Asp to Met

dfdfd

DJFKDJFJDKJFKDJF


10.4: Amino Acid Synthesis

Most amino acids are synthesized from &alpha-ketoacids or &alpha-hydroxy acids (3-phosphoglycerate), and later transaminated from another amino acid (usually glutamate). The enzyme involved in this reaction is an aminotransferase. Glutamate is usually the amino group donor for this reaction: &alpha-ketoacid + glutamate ⇄ amino acid + &alpha-ketoglutarate

Glutamate itself is regenerated by the amination of &alpha-ketoglutarate, catalyzed by Glutamate dehydrogenase:

The carbon skeletons used for the synthesis of amino acids are intermediates of the glycolysis pathway and the citric acid cycle (see table below)

Source of carbon skeleton used for the synthesis of nonessential amino acids
Intermediates of glycolysis
pyruvate is used for the synthesis of glycine, serine, cysteine
3-phosphoglycerate is used for the synthesis of alanine
Intermediates of citric acid cycle
&alpha-ketoglutarate is used for the synthesis of glutamate, glutamine, proline, arginine
oxalacetate is used for the synthesis of aspartate, asparagine

Tyrosine is another amino acid that depends on an essential amino acid as a precursor. In this case, phenylalanine hydroxylase oxidizes phenylalanine to produce tyrosine:

Phenylketonuria is a genetic disorder that results in low levels of the enzyme phenylalanine hydroxylase. This results in the buildup of dietary phenylalanine to potentially toxic levels. Untreated, PKU can lead to intellectual disability, seizures, behavioral problems, and mental disorders. It may also result in a musty smell and lighter skin.

In general, the synthesis of essential amino acids, usually in microorganisms, is much more complex than for the nonessential amino acids and is best left to a full-fledged biochemistry course.


22.2: Biosynthesis of Amino Acids - Biology

All articles published by MDPI are made immediately available worldwide under an open access license. No special permission is required to reuse all or part of the article published by MDPI, including figures and tables. For articles published under an open access Creative Common CC BY license, any part of the article may be reused without permission provided that the original article is clearly cited.

Feature Papers represent the most advanced research with significant potential for high impact in the field. Feature Papers are submitted upon individual invitation or recommendation by the scientific editors and undergo peer review prior to publication.

The Feature Paper can be either an original research article, a substantial novel research study that often involves several techniques or approaches, or a comprehensive review paper with concise and precise updates on the latest progress in the field that systematically reviews the most exciting advances in scientific literature. This type of paper provides an outlook on future directions of research or possible applications.

Editor’s Choice articles are based on recommendations by the scientific editors of MDPI journals from around the world. Editors select a small number of articles recently published in the journal that they believe will be particularly interesting to authors, or important in this field. The aim is to provide a snapshot of some of the most exciting work published in the various research areas of the journal.


The Shikimate Pathway and Aromatic Amino Acid Biosynthesis in Plants

l -Tryptophan, l -phenylalanine, and l -tyrosine are aromatic amino acids (AAAs) that are used for the synthesis of proteins and that in plants also serve as precursors of numerous natural products, such as pigments, alkaloids, hormones, and cell wall components. All three AAAs are derived from the shikimate pathway, to which ≥30% of photosynthetically fixed carbon is directed in vascular plants. Because their biosynthetic pathways have been lost in animal lineages, the AAAs are essential components of the diets of humans, and the enzymes required for their synthesis have been targeted for the development of herbicides. This review highlights recent molecular identification of enzymes of the pathway and summarizes the pathway organization and the transcriptional/posttranscriptional regulation of the AAA biosynthetic network. It also identifies the current limited knowledge of the subcellular compartmentalization and the metabolite transport involved in the plant AAA pathways and discusses metabolic engineering efforts aimed at improving production of the AAA-derived plant natural products.


Amino Acid Definition

An amino acid is a type of organic acid that contains a carboxyl functional group (-COOH) and an amine functional group (-NH2) as well as a side chain (designated as R) that is specific to the individual amino acid. The elements found in all amino acids are carbon, hydrogen, oxygen, and nitrogen, but their side chains may contain other elements as well.

Shorthand notation for amino acids may be either a three-letter abbreviation or a single letter. For example, valine may be indicated by V or val histidine is H or his.

Amino acids may function on their own, but more commonly act as monomers to form larger molecules. Linking a few amino acids together forms peptides, and a chain of many amino acids is called a polypeptide. Polypeptides may be modified and combine to become proteins.

Creation of Proteins

The process of producing proteins based on an RNA template is called translation. It occurs in the ribosomes of cells. There are 22 amino acids involved in protein production. These amino acids are considered to be proteinogenic. In addition to the proteinogenic amino acids, there are some amino acids that are not found in any protein. An example is the neurotransmitter gamma-aminobutyric acid. Typically, nonproteinogenic amino acids function in amino acid metabolism.

The translation of genetic code involves 20 amino acids, which are called canonical amino acids or standard amino acids. For each amino acid, a series of three mRNA residues acts as a codon during translation (the genetic code). The other two amino acids found in proteins are pyrrolysine and selenocysteine. These are specially coded, usually by an mRNA codon that otherwise functions as a stop codon.

Common Misspellings: ammino acid

Examples of Amino Acids: lysine, glycine, tryptophan


Amino Acid Groups

Amino acids can be classified into four general groups based on the properties of the "R" group in each amino acid. Amino acids can be polar, nonpolar, positively charged, or negatively charged. Polar amino acids have "R" groups that are hydrophilic, meaning that they seek contact with aqueous solutions. Nonpolar amino acids are the opposite (hydrophobic) in that they avoid contact with liquid. These interactions play a major role in protein folding and give proteins their 3-D structure. Below is a listing of the 20 amino acids grouped by their "R" group properties. The nonpolar amino acids are hydrophobic, while the remaining groups are hydrophilic.

Nonpolar Amino Acids

  • Ala: Alanine Gly: Glycine Ile: Isoleucine Leu: Leucine
  • Met: Methionine Trp: Tryptophan Phe: Phenylalanine Pro: Proline
  • Val: Valine

Polar Amino Acids

  • Cys: Cysteine Ser: Serine Thr: Threonine
  • Tyr: Tyrosine Asn: Asparagine Gln: Glutamine

Polar Basic Amino Acids (Positively Charged)

Polar Acidic Amino Acids (Negatively Charged)

While amino acids are necessary for life, not all of them can be produced naturally in the body. Of the 20 amino acids, 11 can be produced naturally. These nonessential amino acids are alanine, arginine, asparagine, aspartate, cysteine, glutamate, glutamine, glycine, proline, serine, and tyrosine. With the exception of tyrosine, nonessential amino acids are synthesized from products or intermediates of crucial metabolic pathways. For example, alanine and aspartate are derived from substances produced during cellular respiration. Alanine is synthesized from pyruvate, a product of glycolysis. Aspartate is synthesized from oxaloacetate, an intermediate of the citric acid cycle. Six of the nonessential amino acids (arginine, cysteine, glutamine, glycine, proline, and tyrosine) are considered conditionally essential as dietary supplementation may be required during the course of an illness or in children. Amino acids that can not be produced naturally are called essential amino acids. They are histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. Essential amino acids must be acquired through diet. Common food sources for these amino acids include eggs, soy protein, and whitefish. Unlike humans, plants are capable of synthesizing all 20 amino acids.


Amino Acid Metabolism and Epigenetics

Epigenetic modification can regulate gene expression by activating or inhibiting gene transcription without changing the DNA sequence, ultimately affecting embryonic development, stem cell differentiation, senescence, and tumorigenesis (Brien et al., 2016 Cavalli and Heard, 2019). Epigenetic aberrations, especially DNA methylation, histone modifications, chromatin remodeling, and small RNAs, have been described in malignant hematological and solid tumors and can be considered as common features of cancer development and progression (Sharma and Rando, 2017 Toh et al., 2017 Nebbioso et al., 2018). Tumorigenesis-associated metabolic reprogramming affects the genomic status by regulating the enzymes for epigenetic modifications, which commonly utilize key metabolites as either substrates or allosteric regulators (Etchegaray and Mostoslavsky, 2016 Van Der Knaap and Verrijzer, 2016 Sabari et al., 2017). The chemical modification of DNA and histones is very sensitive to cell metabolism and nutritional status (Su et al., 2016).

DNA methylation refers to the transfer of the methyl group provided by SAM to the 5-position carbon atom of cytosine, catalyzed by methyltransferase (DNMT), to form 5′-methylcytosine. During tumorigenesis, abnormal hypermethylation of the cytosine in CpG islands and hypomethylation of the whole genome result in genome instability and alterations in gene expression profile, including silencing of tumor suppressor genes, endogenous retro-elements, and tumor antigens, and activation of oncogenes (Liang and Weisenberger, 2017 Schorn et al., 2017). Intracellular SAM, the one carbon-derived methyl donor, is synthesized by methionine and ATP in the presence of methionine adenosine transferase (Figure 1). As the main methyl donor in cells, SAM also mediates a variety of methylation reactions, aside from DNA methylation, including histone, RNA, and some protein amino acid residue methylation (Teperino et al., 2010). Uptake and metabolism of folate, vitamins B6 and B12, choline, betaine, serine, and glycine may influence the methyl donor pool, and, ultimately, degrees of methylation modifications (Sapienza and Issa, 2016). LAT1 (SLC7A5) is responsible for inputting essential amino acids, including methionine therefore, LAT1 (SLC7A5) is essential for maintaining the intracellular SAM concentration. The expression of LAT1 is upregulated in many cancers and is associated with poor prognosis (Yanagisawa et al., 2012 Isoda et al., 2014 Shimizu et al., 2015). Downregulation of LAT1 (SLC7A5) suppresses methionine input, thus reducing the level of cellular SAM, resulting in methylation depletion of some histones and inhibition of tumor growth. More importantly, the downregulation of the EZH2 gene leads to a decrease in LAT1 (SLC7A5) expression, and, in turn, the downregulation of LAT1 (SLC7A5) or the depletion of essential amino acids can also induce a decrease in EZH2 expression (Dann et al., 2015). The positive feedback loop of EZH2-LAT1 (SLC7A5) indicates the potential of LAT1 (SLC7A5) as a target for cancer therapy (Hafliger and Charles, 2019).

In addition to regulating epigenetic methylase activity, metabolism also affects epigenetic enzymes involved in demethylation in cancer cells. Through α-KG-dependent dioxygenase, the amino acid metabolite α-KG is also involved in regulating histone and DNA demethylation (Xu et al., 2011 Xiong et al., 2018 Lio et al., 2019). These α-KG-dependent dioxygenases include the Tet family, which catalyzes the conversion of 5-methylcytosine to 5-hydroxymethylcytosine the Jumonji C domain-containing histone demethylase, which catalyzes the demethylation of mono-, bi-, and trimethyl lysine residues by oxidation and the prolyl hydroxylase (PHD) family, which hydroxylates hypoxia-inducible factor (HIF) to mediate its degradation (Wu et al., 2018 Duan et al., 2019 Lio et al., 2019). These reactions require the participation of α-KG, so low levels of α-KG may cause hypermethylation of DNA and histones. IDH mutations were first reported in GBM and were later found in other tumors, such as AML, cholangiocarcinoma, and chondrosarcoma (Parsons et al., 2008 Marcucci et al., 2010 Amary et al., 2011 Borger et al., 2012). Normal IDH catalyzes the dehydrogenation of isocitrate to α-KG. However, when it mutates, IDH converts α-KG to 2-hydroxyglutaric acid (2-HG) and competitively inhibits α-KG-dependent DNA and histone demethylases (Xu et al., 2011), leading to a hypermethylation phenotype and may alter the differentiation of cancer stem cells (Yang et al., 2012 Tommasini-Ghelfi et al., 2019). In IDH1 mutant glioblastoma, BCAT1 is transcriptionally suppressed because of the hypermethylation of three CpGs in the promoter, and this is also the consequence of IDH1 mutation-induced 2-hydroxyglutarate (2-HG) (Tonjes et al., 2013). The suppression of BCAT1 can block glutamate excretion and, thus, leads to reduced growth and invasiveness of glioblastoma (Tonjes et al., 2013). In human AML stem cells, BCAT1 is overexpressed, and the BCAA pathway is activated by the low levels of α-KG, displaying a DNA hypermethylation phenotype similar to IDH mutant-positive cancers (Raffel et al., 2017). Knockdown of BCAT1 causes accumulation of α-KG, promoting EGLN1-mediated HIF1α protein degradation and leukemia-initiating arrest (Raffel et al., 2017). For patients with IDH (WT)/TET2 (WT) myeloid leukemia, a high level of BCAT1 is a strong predictor of worse survival outcomes, and the BCAT1 level significantly increases on disease relapse (Raffel et al., 2017). In recent years, IDH inhibitors targeting IDH mutants, including ivosidenib and enasidenib (Table 1), have been approved by the Food and Drug Administration to be used in patients with IDH1 or IDH2 mutant recurrent or refractory AML, respectively (Kim, 2017 Dhillon, 2018), while trials of IDH inhibitors for other tumors such as cholangiocarcinoma, chondrosarcoma, and myelodysplastic syndrome are still underway (Abou-Alfa et al., 2020 Stein et al., 2020 Tap et al., 2020). Unlike α-KG, abnormal accumulation of succinate and fumarate in tumor tissues represses PHD, thus reducing HIF1 α hydrolysis, suppressing demethylation of DNA and histones, and promoting the occurrence and development of tumors (Cavalli and Heard, 2019). The mutation or decrease in the succinate dehydrogenase (SDH) gene leads to an increase in the concentration of succinate. SDH gene mutations have been confirmed to exist in many tumors, such as gastrointestinal stromal tumors, renal cell carcinoma, pheochromocytoma, and paraganglioma (Pasini and Stratakis, 2009 Dwight et al., 2013 Calio et al., 2017).

Histone post-translational modifications are another set of epigenetic marks in cancers (Audia and Campbell, 2016). Emerging evidence suggests that eight types of Lys acylations on histones affect chromatin structural changes and gene expression (Sabari et al., 2017). Histone acetylation, which is well characterized, is controlled by the opposing activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). HATs catalyze the addition of acetyl groups from the acyl donor acetyl-CoA, which can be produced by glucose, fatty acids, and BCAA metabolism (Figure 1), to lysine residues in histone tails—thus called histone acetylation. Histone acetylation can be regulated by acetyl-CoA from different sources in different cell conditions (Sivanand et al., 2018). HDACs, responsible for the removal of acetyl groups from histone lysine residues, have been reported to have abnormal expression in cancers, and HDAC inhibitors (HDACi) have been considered as potential drugs in cancer treatment (Audia and Campbell, 2016 Li and Seto, 2016 Peleg et al., 2016 San Jose-Eneriz et al., 2019 Mirzaei et al., 2020 Wang P. et al., 2020 Wang X. et al., 2020).

The metabolic reprogramming of cancer cells through amino acids affects epigenetic change. In turn, epigenetic modifications in key enzymes in amino acid metabolism induce the malignant transformation of cells (Blanc and Richard, 2017 Ali et al., 2018). A recent study has shown that argininosuccinate synthase 1 (ASS1) and spermidine/spermine N1-acetyltransferase (SAT1), the central enzymes for arginine metabolism, are hypermethylated in cisplatin-resistant bladder cancer cells (Yeon et al., 2018). Downregulation of ASS1 caused by promoter methylation increases the susceptibility of tumor cells to PEGylated arginine deiminase (ADI-PEG20) (Table 1), a drug for arginine-deprivation treatment that has been used in clinical trials for a variety of tumors (Delage et al., 2012 Syed et al., 2013 Mcalpine et al., 2014). Another recent screening identified that H3K9 demethylation-mediated upregulation of BCAT1 and subsequent BCAA metabolic reprogramming is able to enhance the capacity for sublethal epidermal growth factor receptor (EGFR) inhibitor (TKI) resistance by producing ROS scavengers in lung cancer, which is a cancer where EGFR mutations are commonly found (Wang et al., 2019b).


Protein biosynthesis

Protein biosynthesis (Synthesis) is the process in which cells build proteins.

The term is sometimes used to refer only to protein translation but more often it refers to a multi-step process, beginning with amino acid synthesis and transcription which are then used for translation.

Protein biosynthesis, although very similar, differs between prokaryotes and eukaryotes.

The events following biosynthesis include post-translational modification and protein folding.

During and after synthesis, polypeptide chains often fold to assume, so called, native secondary and tertiary structures.

This is known as protein folding.

Amino acids are the monomers which are polymerized to produce proteins.

Amino acid synthesis is the set of biochemical processes (metabolic pathways) which build the amino acids from carbon sources like glucose.

Not all amino acids may be synthesised by every organism, for example adult humans have to obtain 8 of the 20 amino acids from their diet.

The amino acids are then loaded onto tRNA molecules for use in the process of translation.


Biochemistry notes| PDF | study material

1). Introduction:
2). Definition:
3). Function of Protein
4). Physiochemical properties of proteins
5). Chemical Properties of Proteins
6). Classification of Proteins
7). Amino Acids
8). Structure of a Typical Amino Acid
9). Amino Acids linkage via Peptide Bonds
10). Structure of various Amino acids
11). Classification of Amino acids
12). Physio Chemical Properties of Amino acids:
13). Colour reactions of amino acids
14). Biological importance of amino acids
15). Polypeptide
16). Structure of protein
17). Protein deficiency disease:

Read now

Vitamins and mineral

  • 1). Introduction
  • 2). Classification by food
  • 3). Classification by predominant function
  • 4). Nutrient
  • 5). Protein
  • 6). Function of protein
  • 7). Evolution of protein
  • 8). Assessment of protein nuclear status
  • 9). Fat
  • 10). Fat fatty acid and hydrolysis
  • 11). Function of fats
  • 12). Carbohydrate
  • 13). Dietary fibres
  • 14). Vitamins
  • 15). Vitamin a, function of vitamin a
  • 16). vitamin d, function of vitamin d
  • 17). Thymine
  • 18). Vitamin b6 and vitamin b12
  • 19). Vitamin b12 deficiency
  • 20). Vitamin c
  • 21). Malnutrition
  • 22). kwashiorkor, symptoms
  • 23). marasmus, symptoms
  • 24). Mineral, anaemia

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Metabolism

  • 1). Introduction
  • • Anabolic pathways
  • • Catabolic pathways
  • • Amphibolic pathways
  • 2). Carbohydrate Metabolism
  • 3). Lipid Metabolism
  • 4). Amino Acid Metabolism

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Lipids and lipid metabolism

  • 1). Fatty acids
  • 2). Triacylglycerol
  • 3). Phospholipids
  • 4). Steroids
  • 5). Lipid metabolism
  • 6). Oxidation of fatty acids
  • 7). Biosynthesis of fatty acids
  • 8). Cholesterol synthesis

Read now

Enzyme

  • 1). Chemistry
  • 2). Classification
  • 3). Mechanism of EnzymeAction
  • 4). Enzyme Kinetics
  • 5). Inhibition
  • 6). Activation
  • 7). Specificity
  • 8). Introduction
  • 9). Structure of enzyme
  • 10). Cofactor
  • 11). Acid base crystallizer
  • 12). Crystallized by proximity
  • 13). Lock and key model
  • 14). Effect of PH
  • 15). Michaelis-Menten Equation
  • 14). ASSUMPTIONS FOR
  • 15). MICHAELIS-MENTEN EQUATION INHIBITORS
  • 16). TYPES OF REVERSIBLE INHIBITION
  • 17).EXAMPLES OF UNCOMPETITIVE INHIBITION
  • 18). MIXED INHIBITION
  • 19). Activation by co-factors
  • . 20). Conversion of an enzyme precursor
  • . 21). GROUP SPECIFICITY
  • 22). BOND SPECIFICITY
  • 25). OPTICAL / STEREO-SPECIFICITY
  • 26). DUAL SPECIFICITY

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Enzyme

1). Oxido-reductases
2). Transferase 3). Hydrolases
4). Lyases
5). Isomerases
6). Ligases
7). FACTOR AFFECTING ENZYME ACTIVITY
8). ENZYME INHIBITION
• Competitive inhibition
Non-competitive inhibition
9). DIAGNOSTIC APPLICATION OF ENZYMES


22.2: Biosynthesis of Amino Acids - Biology

All articles published by MDPI are made immediately available worldwide under an open access license. No special permission is required to reuse all or part of the article published by MDPI, including figures and tables. For articles published under an open access Creative Common CC BY license, any part of the article may be reused without permission provided that the original article is clearly cited.

Feature Papers represent the most advanced research with significant potential for high impact in the field. Feature Papers are submitted upon individual invitation or recommendation by the scientific editors and undergo peer review prior to publication.

The Feature Paper can be either an original research article, a substantial novel research study that often involves several techniques or approaches, or a comprehensive review paper with concise and precise updates on the latest progress in the field that systematically reviews the most exciting advances in scientific literature. This type of paper provides an outlook on future directions of research or possible applications.

Editor’s Choice articles are based on recommendations by the scientific editors of MDPI journals from around the world. Editors select a small number of articles recently published in the journal that they believe will be particularly interesting to authors, or important in this field. The aim is to provide a snapshot of some of the most exciting work published in the various research areas of the journal.


Watch the video: Chapter 22 Biosynthesis of Amino Acids (May 2022).


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