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Slide 1
Slide 1

... with some differences: • RNA molecule is single-stranded (rather than double stranded in DNA) • Uracil instead of Thymine. So in RNA Adenine binds with Uracil ...
Chapter 6, Section 3
Chapter 6, Section 3

... Enzymes act on specific substrates ◦ Substrate: substance that the enzyme breaks down  Each substrate fits into the active site. (Like a lock & key) ...
Macromolecule Matching
Macromolecule Matching

... B. Nucleic Acid C. Carbohydrate D. Lipid 18 | P a g e ...
chapter3_part2
chapter3_part2

... coiled (helical) or sheetlike array held in place by hydrogen bonds (dotted lines) between different parts of the polypeptide chain. ...
Nonessential Amino Acid Metabolism in Healthy Adult Males Using
Nonessential Amino Acid Metabolism in Healthy Adult Males Using

...  Rose et al. (1948) showed increased growth by 7075% in rats fed essential amino acids (EAA) + NEAA  Rechcigl et al. (1957) showed different growth rates in rats  Glutamate gave the largest increase in growth  Followed by Alanine, Aspartate, Asparagine, Proline, and Glutamine  Smallest increase ...
Chapter 25
Chapter 25

... phosphorylated form, NRI-P • NRI is phosphorylated by NRII, a protein kinase • If NRII is complexed with PIIA it acts as a phosphatase, not a kinase ...
Structural basis for the functional differences between ASCT1 and
Structural basis for the functional differences between ASCT1 and

... The alanine, serine and cysteine transporters (ASCT1 and 2) are electroneutral exchangers. They belong to the Solute Carrier Family 1, along with human glutamate transporters (Excitatory Amino Acid Transporters EAATs). Neutral amino acid exchange via ASCT1 is thought to be coupled to only one Na+ io ...
LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034 Part A
LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034 Part A

... 11. Bring out the biochemistry of co-enzymes. 12. Explain the reaction characteristics of proteins. 13. Describe the process of catabolism of amino acids. 14. Bring out the biosynthetic pathways of cholesterol and bile. 15. Explain the process and importance of electron transport chain. 16. Describe ...
Building Monomers of Macromolecules
Building Monomers of Macromolecules

... 12. What element is found in amino acid that isn’t found in simple sugars like glucose or fructose? __________________ 13. Amino acids join together to make what type of macromolecule? _________________ 14. What are some of the functions of proteins in the body? A. B. C. D. ...
Organic Molecules
Organic Molecules

... Monomers ...
Protein Synthesis
Protein Synthesis

... hydrogen bonds by the enzyme Helicase. This occurs in the nucleus of the cell. Another enzyme, RNA polymerase, then binds to one unwound chain and the gene is transcribed into RNA (transcription). During transcription the triplet-codes of DNA, consisting of three nucleotides, are copied and correspo ...
Macromolecules - Issaquah Connect
Macromolecules - Issaquah Connect

Nuclease Digestion
Nuclease Digestion

Biomolecules Fill in the crossword puzzle by using
Biomolecules Fill in the crossword puzzle by using

... contains the elements carbon, hydrogen,oxygen and nitrogen and is composed of amino acids examples are insulin,hemglobin and enzymes. are the small building blocks of polymers ...
NME2.35: amino acid and protein metabolism 13/03/08
NME2.35: amino acid and protein metabolism 13/03/08

... o Urea has the chemical structure H2N-C(=O)-NH2 o It is responsible for 90% of nitrogen excretion – 45g urea per day o It is water-soluble and an efficient nitrogen carrier (50% weight is nitrogen) o Its formation utilises both cytosolic and mitochondrial space The urea cycle consumes 3ATP and uses: ...
Southern Blot
Southern Blot

... CCU = proline PRO CCC = proline CCA = proline CCG = proline ACU = threonine THR ACC = threonine ACA = threonine ACG = threonine GCU = alanine ALA GCC = alanine GCA = alanine GCG = alanine UGU = cysteine UGC = cysteine UGA = stop UGG = tryptophan CGU = arginine CGC = arginine CGA = arginine CGG = arg ...
proteins - SD57 Mail
proteins - SD57 Mail

... • Ex. Keratin in hair and nails; collagen in skin; actin and myosin in muscle ...
Southern Blot
Southern Blot

... CCU = proline PRO CCC = proline CCA = proline CCG = proline ACU = threonine THR ACC = threonine ACA = threonine ACG = threonine GCU = alanine ALA GCC = alanine GCA = alanine GCG = alanine UGU = cysteine UGC = cysteine UGA = stop UGG = tryptophan CGU = arginine CGC = arginine CGA = arginine CGG = arg ...
File
File

Document
Document

...  Polymer: long chains of monomers Synthesizing and Digesting Polymers  Dehydration Synthesis: removing a water molecule from 2 or more monomers to make a polymer  Hydrolysis: adding water to a polymer to split it apart into ...
(C)
(C)

... 28. The term ketogenic amino acids refers to amino acids: (A) that are precursors for glucose synthesis, (B) degraded to yield acetyl CoA or acetoacetate, (C) that can not be converted to fatty acids or ketone bodies, (D) degraded to yield succinyl-CoA, pyruvate, a-ketoglutarate, fumarate and oxaloa ...
glutamate - Dental Decks
glutamate - Dental Decks

Biochemistry
Biochemistry

...  Amount of substrate or enzyme ...
Ch 18
Ch 18

... ammonia is key—synthesis of most amino acids – Glutamine synthetase incorporates amino group – Coupled to glutamate synthase: reductive  amination of ‐ketoglutarate to glutamate ...
Ch.24Pt.7_000
Ch.24Pt.7_000

... • Describe how a.a. Carbon Skeletons are processed • Define and explain Amino Acid Biosynthesis. • Describe the chemical composition of urine. • Explain the relationship and importance of Arginine, ...
< 1 ... 600 601 602 603 604 605 606 607 608 ... 622 >

Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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