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Topic4-8 :, structure and function of nucleic acids, fxz - Coggle Diagram
Topic4-8 :
Enzyme
Enzyme Structure
Simple enzyme : มีเอนไซม์อย่างเดียวสามารถทำงานได้เลย
Conjugated enzyme : ต้องมี Coenzyme/Cofactor มาจับกับ Apoenzyme
Prosthetic groups, Cofactors and Coenzymes พวกนี้ไม่ใช่โปรตีนแต่ต้องมาจับกับเอนไซม์เพื่อให้เอนไซม์ทำงานได้
Cofactors
จำพวกไอออน จะเป็นการจับแบบ reversibly (สามารถย้อนกลับได้)
Coenzymes
Most of them are water soluble vitamins, if the body lacks vitamins, the enzymes do not work well.
Prosthetic groups
•Tight, stable incorporation into a protein’s structure by covalent or non-covalent
forces.
•Pyridoxal phosphate, flavine mononucleotide (FMN), Co, Cu, Fe, Mg, Mn and Zn
ได้แก่ Co,Cu,Fe,Mg,Mn and Zn
Apoenzyme คือ เอนไซม์ที่ยังไม่ได้ไปจับกับ Coenzyme / Cofactor
Factors Affecting Enzyme Activity
pH
Reaction time
Temperature
Activators and Inhibitor
Enzyme concentration
Covalent modification
Substrate concentration
Enzyme Classification and Enzyme Nomenclature
Enzyme Classification
Hydrolases
The function is Works in reactions that require water. Most of them are enzymes in the digestive system.
Lyases
The function is about functional groups are added and removed to form double bonds.
Transferases
The function is การเคลื่อนย้ายหมู่ฟังก์ชั่น substrate ให้กลายเป็น product
Isomerases
The function is transform the structure into an isomer
Oxidoreductases
The function is Oxidation and reduction
Ligases
The function is to connect 2 substrates and this activity need ATP
Enzyme Nomenclature
Prefix : describe function of enzyme
Oxidase , Hydrolase
Substrate + function of enzyme
โดยตัวแรกจะบอก Substrate ตัวหลังจะบอกถึงฟังก์ชั่น
Glucose oxedase
Alcohol dehydrogenase
Suffix
-ase : Urease, Sucrase, Lipase
-in : Trypsin, Chymotrypsin, Pepsin
Allosteric Enzymes
• Enzymes with multiple subunits, with each subunit
working together
Allosteric site for Inhibitor or Activator
Inhibitor and activator that capture the Allosteric site will cause a catalyst or inhibit the reaction. depending on the catcher
Definition of enzyme and How enzymes works ?
Most of the enzymes are proteins
Enzymes are specific proteins that accelerate the speed of chemical
reactions in the body
work of enzymes
Induce Fit model
Conformational changes are occurring at the active site of enzymes
concomitant with the combination of enzyme with the substrate
Lock and Key model
Enzyme and substrate fit each other
Enzyme Applications
Medical
produce the drugs
Disease indicators
environmental
Enzymes are used to break down plastics.
Industrial
Bakery industry
Juice production industry
Kinetic parameters
Km : The affinity of the enzyme to the substrate
Low Km :Enzyme binds well to the substrate
High Km : Enzyme poorly binds to the substrate.
Vmax
The rate of reaction when the enzyme is saturated with substrate is the maximum rate of reaction.
Depend on the amount of enzyme
Powerful enzyme
Low Km
High Vmax
Hih Kcat
Kcat
Kcat : Enzyme efficiency
โครงสร้างและหน้าที่ของกรดอะมิโนและโปรตีน(structure and function of proteins)
General structure of an amino acid
consist of amino group a carbon group
side chian amino can change by side chain
classification of amino acids
classification based on properties of R groups
nonpolarr aliphatic R groups
polar uncharged R groups
positively changed R groups
negative charged R groups
non polar aromatic R groups
classification based on structure
1 Aliphatic amino acids
mono amino mono carboxylic acids
simple amino acids
Branched chain amino acids
Hydroxy amino acids
Sulphur containing amino acids
Amino acids with amide group
Mono amino dicarboxylic acids
Di basic mono carboxylic acids
2 Aromatic amino acids
Phenylalanine, Tyrosine
3 Heterocyclic amino acids
Tryptophan, Histidine
4 Imino acid
Imino acid
Classification of Amino Acids based on Nutritional Requirements
Essential or Indispensable amino acids
Isoleucine, Leucine, Threonine, Lysine, Methionine, Phenylalanine, Tryptophan, Valine : Their carbon skeleton cannot be synthesized by human beings and so preformed amino acids are to be taken in food for normal growth
Partially essential or Semi-essential
amino acids
Histidine and arginine : Growing children require them in food but they are not essential for the adult individual
Nonessential
Cysteine, Glycine, Serine, Alanine, Tyrosine, Asparagine, Aspartate, Glutamine, Glutamate, Proline : their carbon skeleton can be synthesized by the body
Chemical and Physical Properties of Amino Acids
Acid-Base and Buffer Properties of Amino Acids
The breakdown of carboxylic and amino groups makes amino acids a Zwitterion (German word "zwitter" = hybrid) or dipolar ion in solution, depending on the pH of the medium
Amino acids = Amphoteric Compound
physiological pH of 7.4, both carboxyl and amino groups of amino
acids are completely ionized
Isoelectric point or pI
The pH at which the
molecule carries no net charge
Solubility and buffering
capacity will be minimum at iso-electric pH
No mobility in an electrical field
Optical Activity
Amino acids having an asymmetric carbon atom exhibit optical activity: D
and L isomers
The L-amino acids occur in nature Natural amino acids
General Reactions of Amino Acids
Due to Carboxyl Group
Decarboxylation
Amide formation
Reactions Due to Amino Group
Transamination
Oxidative deamination
Formation of carbamino compound
Reactions Due to Side Chains
Transmethylation
Ester formation by the OH group
Reaction of the amide group
Reactions of SH group
Peptide Bond Formation
Covalently join the alfa-carboxyl group (-COOH) of each amino acid to the alfa-amino group (-NH2) of another by dehydration or condensation reaction
Atoms in peptide bond from a rigid, planar unit
Peptide bond has no freedom of rotation
Protein Structure
Primary structure
three dimensional arrangement
Secondary structure
Regular arrangements in space of adjacent amino acid residues in a polypeptide chain e.g. alfa helix and beta conformation
Tertiary structure
Amino acid sequence of polypeptides linking with peptide bond
Quaternary structure
The overall spatial arrangement of poly peptides or subunits, within the protein
Classification of Protein
Solubility properties
Soluble in water
Insoluble in water
Chemical composition
Simple proteins
Conjugated proteins
Protein configuration
Fibrous proteins
Globular proteins
Biological functions
Structural proteins
Silk, Collagen, Elastin
Storage proteins
Ovalalbumin, Casein
Transport proteins
Hemoglobin
Hormonal proteins
Insulin
Regulator proteins
Membrane proteins
Contractile proteins
Actin & Myosins
Defensive proteins
Antibodies
Enzymatic protein
DNA polymerase
Structure and
function of carbohydrates
Chemical Properties of Monosaccharides and Their Derivatives
Oxidation
Reduction
Enediol Formation
Glycosidation
Epimerization “Epimerism of Aldoses”
Phosphorylation: Kinase + ATP
Mutarotation “Anomerism of Sugars”
Structure and Chemical Bonding of Oligosaccharides and Polysaccharides
2.Oligosaccharide: Monosaccharides (2-15 molecules) covalently
link together with glycosidic bond
Maltose
Glucose + Glucose
Lactose
Galactose + Glucose
Sucrose
Glucose + Fructose
Polysaccharide (glycan)
Homopolysaccharides:
Glycogen
Cellulose
Starch
Chitin
Heteropolysaccharides
Peptidoglycan (N-acetyl-D-glucosamine +N-acetylmuramic acid)
Glycoaminoglycan
Type of Carbohydrate and Classification
Oligosaccharide
sucrose
maltose
lactose
Polysaccharide
amylose
amylopectin
glycogen
cellulose
Monosaccharide
Aldose(-CHO)
Ketone(-C=O)
Stereochemical Structure and Nomenclature of Monosaccharides
Relationship of Glycohemoglobin with Blood Glucose Levels
structure and function of nucleic acids
infrastructure nitrogenous base types pyrimidine and purine
(Pyrimidine)
Togerther with = cytosine(c),tymine(t)
(Purine)=adeine(a),guanie (g)
Pentose sugar is a constituent of nucleic acids.
(Deoxyribose) component of (DNA)
(Ribose) component of (RNA)
Nucleotides and Nucleosides
Nucleotide there are 5 types
Contains nucleic acids and phsphate groups
Nucleoside =substances made up of bases and pentose
Structure and types of nucleic acids
Structure
Sugar with 5 carbon atoms
ribose
deoxyribose
Phosphate group
nitrogenous base
Types
1.DNA(deoxyribonucleic acid)
2.RNA(ribonucleic acild)
The double helix structure of nucleic acids.
The DNA double helix is a spiral polymer of nucleic acids.
These are linked together by nucleotides. in B-DNA
Chemical and physical properties of nucleic acids
Chemical properties=DNA is normally acidic because of phosphate
physical properties =Absorbtion 260nm
DNA, Genes and Chromosomes
DNA= is made up of two long strands of polymer made up of subunits called nucleotides, with a sugar core and a phosphate group connected by ester bonds.
DNA inside cells is organized into long structures called chromosomes.
Gene= is a genetic unit located on a chromosome. It is an essential component of nucleic acids known as DNA.
There are two types of genes: autosome genes and sex chromosome genes.
Chromosomes are the storage of genetic units. which controls a and transmits information about various genetic characteristics of living things
Biological functions of nucleic acids
Biosyn thesis pathway:S-adenosylmethionine
Energy storage :Adenosine 5-triphosphate(ATP)
Genetic information : RNA and DNA
Singnaling molecule:Adenosine 3’-5’-cyclic-monophosphate
Ennzyme regulation :ATP,GTP,NADH
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