Anabolic Pathways and Synthesis - Biochemistry

The DH subunit is a dehydratase, meaning it removes alcohol groups from carbon chains. If this subunit is mutated, the alcohol cannot be removed.

Because acetyl-CoA Carboxylase (ACC) is directly responsible for synthesis of malonyl-CoA, inhibiting it would be the most targeted approach. Inhibiting acyl-CoA dehydrogenase or pyruvate dehydrogenase would decrease available acetyl-CoA to ACC by inhibiting beta-oxidation and conversion of pyruvate to acetyl-CoA, but this would have a large impact on other biosynthetic pathways as well, due to the ubiquity of acetyl-CoA.

-hydroxybutyrate dehydrogenase catalyzes the interconversion of the ketone bodies acetoacetate and -hydroxybutyrate, which are transported out of liver cells into the blood to be used as fuel by the rest of the body, particularly during times of starvation. -hydroxybutyrate dehydrogenase’s only coenzyme is . As for the other answers: the pyruvate dehydrogenase complex converts pyruvate into acetyl-CoA, the key connection between glycolysis and the citric acid cycle, and this process uses a number of co-factors, including , thiamine pyrophosphate, lipoamide (the protein-bound form of lipoic acid), and, of course, coenzyme A (to make acetyl-CoA). Pyruvate dehydrogenase uses and depending on the cell type.

The endogenous, not the exogenous, pathway, involves the transformation of VDLDs into LDLs. Meanwhile, the exogenous, not the endogenous, pathway, involves transforming chylomicrons into remnants. The apolipoprotein in plasma (transporting cholesterol to the liver) which is the major component of HDL is A1, not B100. Macrophages do indeed oxidize LDLs and transform themselves into the foam cells which indicate atherosclerosis. This is one of the reasons that LDL cholesterol levels can indicate atherosclerosis (which is associated with increased risk of heart attack or stroke).

Acyl-Carrier Protein (ACP) is a protein that is important to the generation of lipids. Specifically, it aids in the production of fatty acids. Furthermore, ACP is just one component of the Fatty Acid Synthase enzyme, which is devoted to the synthesis of fatty acids.

To begin the process, ACP is first activated by having an acetyl-CoA molecule attached to it. Next, a compound called malonyl-CoA is attached to the bound acetyl-CoA. Malonyl-CoA is a three carbon compound, but upon being added to the acetyl-CoA, the malonyl-CoA becomes decarboxylated. The importance of this is that by producing carbon dioxide as a product, this helps to greatly drive the reaction forward.

Keep in mind that there are other chemical transformations happening when these malonyl-CoA molecules are being "stitched" together. Every time a malonyl-CoA is added, the carbon chain becomes increased by two more carbons. This keeps happening until, finally, a fatty acid is generated.

Lecithin-cholesterol acyltransferase-LCAT adds a fatty acid to cholesterol, which can then be loaded onto high-density lipoproteins. Without the enzyme, cholesterol does not get to be transported by high density lipoproteins to the liver. Cholesterol then accumulates in tissue such as the eye and renal tissue. LCAT does impact cholesterol transport. Lipoprotein lipase is the enzyme that hydrolyzes fatty acids from triglycerides and cholesterol. Fatty acid synthase converts malonyl-CoA into palmitate. Acetyl-CoA carboxylase is the enzyme that incorporates acetyl-CoA into fatty acids.

Fatty acid desaturases are located on the endoplasmic reticulum and convert saturated fatty acids to unsaturated fatty acids by producing double bonds. The enzymes have a N-terminal cytochrome b5-like domain. Arachidonic acid is a highly unsaturated fatty acid.

Citrate crosses the mitochondrial matrix into the cytosol and is converted into acetyl-CoA and oxaloacetate by citrate lyase during fatty acid synthesis, as part of the citrate shuttle. The process requires hydrolysis of energy-rich ATP bonds.

The role of fatty acid synthase is to synthesize fatty acids,more specifically to convert acetyl-CoA, malonyl-CoA, and NADPH to palmitate (a fatty acid) and NADP. It is a multienzyme complex consisting of 7 components: acetyl CoA-ACP transacetylase, malonyl-CoA-ACP transacetylase, Beta-ketoacyl synthase, Beta-ketoacyl reductase, Beta-hydroxyacyl dehydratase, enoyl reductase, thioesterase.

The pentose phosphate pathway (also known as the hexose monophosphate shunt or HMS), which mainly serves to produce for anabolic reduction reactions and ribose-5-phosphate for nucleic acid production, takes place in the cytosol of hepatic cells.

Scientists have indeed counted about 20,000 proteins coded for by the genome. Coding sequences are only about 2% or less of the genome. The definition of paralogs is genes related by duplication within a genome. Within the genome, not about 5%, but rather about 50%, of DNA sequences are repeated.

From the carbon skeleton of oxaloacetate, methionine can be created. However, glutamine comes from alpha ketoglutarate, valine and leucine come from pyruvate, and histidine comes from ribose-5-phosphate.

The reaction for the conversion of glutamine into glutamate is:

As seen in the reaction above, carbon dioxide is uninvolved.

When a change results in an early stop codon, nonsense mutation occurs and the protein is done being read early, often resulting in a nonfunctional protein. When a base change results into a different amino acid, this is a missense mutation. When a base change occurs but results in the same amino acid being read, this is considered a silent mutation.

Just as there is an initiation codon regulating translation, there are termination codons that code for the end of translation. The three termination codons are UAA, UAG, and UGA.

A helpful mnemonic for these are the phrases:

You are annoying (UAA)

You are gross (UAG)

You go away (UGA)

To answer this question, it's essential to have an understanding of what a signal sequence is.

A signal sequence (also sometimes called a signal peptide) is a specific sequence of amino acids on a polypeptide that appears near the beginning of translation. When this signal sequence is present, it causes a temporary halt in the translation process. Meanwhile, another protein called a signal recognition particle (SRP) comes along and binds to the ribosome that is translating the polypeptide. Together, this polypeptide-ribosome-SRP complex is transferred from the cytosol to the surface of the endoplasmic reticulum (ER). Once there, the complex allows the polypeptide to resume synthesis, but in doing so, causes it to be synthesized into the inner lumen of the endoplasmic reticulum. Consequently, this polypeptide will go on to be modified within the ER and also the Golgi apparatus. Afterwards, it will be sent off within a vesicle, where is will either be A) secreted outside of the cell or B) incorporated into the endomembrane system of the cell (in other words, the peptide will be inserted into a membrane such as the plasma membrane, ER membrane, Golgi membrane, etc.). Lastly, it is the nuclear localization sequence (NLS) that, when added to a protein, allows it to enter the nucleus through the nuclear membrane.

Procollagen has amino and carboxy procollagen extension propeptides that make it soluble. The preprocollagen undergoes both hydroxylation and glycosylation at specific aminoacid residues to form procollagen. Once secreted extracellularly, proteinases remove the extension peptides from procollagen to form the final collagen molecule.

Biotin moves carboxyl groups in the enzyme acetyl-CoA carboxylase. Tetrahydrofolate and S-adenylosyl methionine move methyl groups in amino acid synthesis and post-translational modifications such as DNA methylation. B12 cobalamin is a cofactor in the reactions producing succinyl-CoA and methionine, where it transfers methyl groups to complete the products.

Transcription is the second process involved in the production of proteins from a gene. The three processes are DNA replication, transcription, and translation. DNA replication involves replication of DNA from a parent strand, transcription involves the synthesis of a RNA molecule from a DNA molecule, and translation involves the conversion of the mRNA molecule to a polypeptide.

As mentioned, transcription produces an RNA molecule from a DNA molecule (parent strand). Recall that RNA molecules have uracil, whereas DNA molecules have thymine; therefore, the product will contain more uracil.

Amino acids are found in proteins. Since the products of transcription are nucleic acids (RNA molecules) they won’t contain any amino acids. Recall that a nucleic acid consists of pentose sugar molecules (ribose in RNA and deoxyribose in DNA), nitrogenous bases (adenine, guanine, cytosine, thymine (in DNA), and uracil (in RNA)), and phosphate groups.

RNA polymerase is an important enzyme involved in transcription. Its function is to add nucleotides to the growing mRNA chain. Although it adds complementary nucleotides to the DNA, RNA polymerase itself doesn’t bind to complementary DNA sequences, rather it binds at promoters.

There are three types of RNA molecules. First, mRNA molecules are the main products of transcription that undergo translation to produce most of the proteins found in a cell. Second, tRNA molecules are special RNA molecules that facilitate the addition of amino acids to a growing polypeptide chain during translation. Third, rRNA molecules are components of ribosomes and are synthesized in the nucleolus (location of assembly of ribosomes). The enzyme in this question is involved in the production of rRNA molecules. RNA polymerase I is used in production of rRNA molecules. RNA polymerase II is used for mRNA molecules and RNA polymerase III is used for tRNA molecules.