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Disaccharides: 2 sugars
Polysaccharides: many sugars
Monosaccharides: simple sugars
Lactose: galactose & glucose rings connected via 1,4 glycosidic linkage
Homoglycans: storage compounds consisting of glucose that can be released via hydrolysis
Heteropolysaccharides: more than on sugar type, Nlinked or O-linked attached to proteins; Asn, Ser, or Thr residues
Glycosaminoglycans (GAGs): high negative charge, binds water, provides cushion. Repeating disaccharide units
Glucose: primary energy source; 6 carbon aldo sugar
Maltose: 2 glucose rings, 1,4 alpha linkage
starch: consists of amylose (not branched, a1,4, plants) amylopectin (branched every 20-25, a1,4 and a1,6, plants)
N-linked: B-glycosidic bond to side chain amide nitrogen of asparagines
Fructose: sweeter than glucose; 6 carbon keto
Sucrose: glucose and fructose, 1-->2 linkage
Glycogen: branched every 8, a 1,4 a1,6, animals muscle liver
O-Linked: attached through serine or threonine residues.
Galactose: combined with glucose to make lactose; 6 carbon aldo
Cellobiose: 2 glucose, 1,4 linkage
Cellulose: not branched, long linear chains of glucose, B1,4 hydrogen bonds, plant cell walls
Glyceraldehyde: smallest sugar; 3 carbon aldo
Ribose: 5 carbon aldo
D-Glucose to DFructose Esterification: hydroxyl groups react with an acid to make an ester.anomers Epimers: differ in configuration about one carbon D-Glucose & D Fructose Nomenclature: [C(H2O)]n. Aldehyde to hemiacetal to acetal and water. . aldehydes CHO on 1st carbon. D=OH on right. alpha & Beta a-glucose & bglucose Epimerization: isomerization where configuration about a chiral carbon. Ketone to hemiketal to ketal and water Glycosylation: sugars react with proteins and lipids to form Nglycosidic or O-glycosidic bonds. Glucose + ATP --> Glucose-6-phosphate Reactivity: Glycoside formation: sugars and alcohols to form glycosides. L=OH on left D-Ribose & L-Ribose Stereochemistry: Diastereomers: nonsuperimposable mirror images L-Ribose & LArabinose CARBS Mutarotation: interconversion of alpha and beta isomers.Stereoisomers: chiral carbon atoms. Van't Hoff's rule: number of stereoisomers = 2^n Enantiomers: non superimposable mirror images D&L D or L: chiral carbon furthest from aldo ro keto group. ketone CHO not on 1st carbon Anomer: isomers differ about conformation of anomeric carbon.
Ser. His.kicks in to release COOH end His donates its H+ to Ser Step 6 carboxyl end of substrate released. leaves active site enzymes returns to original state Step 1: Covalent Catalysis Step 3: Electrostatic Effects Step 5: Covalent Bonding .--> Ser and -CH3OH attacks alpha C=O His stabilizes Ser: CH3OH-H------His Step 2 first tetrahedral intermediate formed Ser bound to C=O Lone pairs on O. which opens up a channel for H2O His releases its H+ to the amino group Step 4: Acid/Base Catalysis H2O comes in and acts Nu: His holds the water in its correct location so the -OH can attack the alpha C=O second tetrahedral intermediate formed e. Asp Nu:.from O. kick back in while peptide bond is cleaved COOH end still attached release of amino end & it diffuses away.
IRREVERSIBLE BOND CLEAVAGE: activates enzymes. Ki: E + I x EI ES + I <-> ESI . Tyr side chains common. ATP phosphorylating agent. Vmax decreases Km no change Ki: E + I <-->EI & ES + I <->ESI UNCOMPETATIVE: bind to enzyme-substrate comples. reduce amount of active enzyme REVERSIBLE: Phosphorylation of Ser. Thr. no change in Vmax. Ki=[E][I]/[EI] SEQUENTIAL: substrates independently go through conformational changes. inhibitor competes for active site. apparent change in Km. can occur by induction of synthesis or repression COVALENT MODIFICATION: attaching smal molecles to enzyme to increase or decrease activity.ENZYMES REGULATION INHIBITION GENETIC CONTROL: regulates synthesis and amount of enzyme. substrate binding doesnt displace inhibitor. ex. effective at high [S]. chymotrypsin is synthesized as inactive precursor zymogen ALLOSTERIC: cooperativitybinding of first substrate increases affinity for binding of other substrates IRREVERSIBLE: result from covalent bonds with an amino acid side chain in the enzyme active site. T state binds weak ex: O2 binding to hemoglobin COMPETITIVE: substrate/inhibitor structurally similar. affinity increases each bond NONCOMPETITIVE:bind to site other than active site. phosphate group hydrolyzed in rxn catalyzed by phosphatases zymogen activated via peptide bond cleavage CONCERTED: all subunits change conformation at once. R state binds tight. Kinases catalyze rxn . Km and Vmax decrease. Control over timing of enzyme synthesis.
vo=Vmax/2 . [S]>>[E]. Kf/Kr=[B]^m/[A]^n=Keq A + B --> C.Grcts= G° EQUILIBRIUM: catalysts effect rate but not Keq A-->B . vo=Vmax[S]/Km [S]=Km. k units 1/time. Gpdts. first order reaction Km: measure of affinit between enzyme and substrate. lower Km value. v=k[A]. second order reaction. as [B] increases [A] decreases. vo= Vmax [S]<<Km. k units M^-1 s^-1 Vmax=Kcat[E]t. Kf: forward rate. higher barrier slower rxn. v= dB/dt=-dA/dt . Kcat is turnover number [S]>>Km. lowered by catalysts FREE ENERGY: large amounts of catalysts change G. lower [S] required to reach half Vmax Km= K-1 + K2/ K1 Vo=Vmax[S]/Km + [S] Kf[A] = Kr[B]. measures direction and extent of rxn. Kr: reverse rate.KINTETICS THERMODYNAMICS Rate: (or velocity) is change per unit of time Michaelis-Menten: assume no reverse reaction. steady state [ES]=constant ACTIVATION ENERGY: determines rate of rxn. v=k[A][B].
or acidic amino aicdside chains donate or accept protons coenzymes. FAD. INORGANIC: required minerals. INDUCED-FIT MODEL: ELECTROSTATIC EFFECTS: effect rxn rate. basic. functional groups initiate rxn. water shields molecules from directly interacting and reduces electrostatic effects. highenergy transfer potential (NAD. less effective ORGANIC: vitamins. metal ion catalysis (Zn+2. NADP-. non protein component Lock and Key: enzyme/substrate binding theory. Fe+2. not as specific to substrate. coenzymes. FMN) APOENZYME: enzyme in absence of cofactor Active Site: site where substrate binds to enzyme. COFACTORS: required for enzymes to function. shielding from a solvent. speed up rxn 10^20 PROSTHETIC GROUPS: tightly bound cofactors.CATALYSIS: enhances rate of rxn but is not permanently altered HIGH CATALYTIC RATE FACTORS ENZYMES: catalyze biochemical rxns PROXIMITY AND STRAIN: substrate molecule is brought into close proximity to reactive specieces in active site. Cu+2) Lewis Acids. conformation change HOLOENZYME: enzyme with cofactor bound COVALENT CATALYSIS: amino acid residues on active site may form covalent bonds with substrate. highly specific ACID BASE CATALYSIS: nonpolar. e. +NH4 groups .& group transfer. -OH groups (serine threonine).