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CU Denver - Chemistry 4810 - Study Guide - Final

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CU Denver - Chemistry 4810 - Study Guide - Final

School: University of Colorado Denver
Department: OTHER
Course: General Biochemistry I
Professor: Jeff Knight
Term: Fall 2017
Tags:
Name: Biochemistry 1 Study Guide III
Description: Enzymes, Kinetics, Carbohydrates, Nucleic Acids
Uploaded: 11/12/2017
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Join more than 18,000+ college students at University of Colorado Denver who use StudySoup to get ahead
School: University of Colorado Denver
Department: OTHER
Course: General Biochemistry I
Professor: Jeff Knight
Term: Fall 2017
Tags:
Name: Biochemistry 1 Study Guide III
Description: Enzymes, Kinetics, Carbohydrates, Nucleic Acids
Uploaded: 11/12/2017
11 Pages 43 Views 34 Unlocks
  • Better Grades Guarantee
  • 24/7 Homework help
  • Notes, Study Guides, Flashcards + More!

Unformatted text preview: Serine Covalent catalysis Transition stgic. Theory - Transient cova lott bond - Highest free chargy state wl enzyme & substrate between reactants & products - e.g. phosphorylation - Least populated state - Must have a hud.cophile. - difficult to advally detect - Alte indicates Sportfancity Thiolate *anything wa negative change of raction Amine. - CATALYSTS do NOT change lonk pair Carboxy AG% A-B=> A+B - AG* '1s the rate of the step - Large aG* : slower rx Chighet 4G"), A-B+XA-+B-- AtX1B - this is the reste determining step huuleophiles dedrophiles * Large dagger, slow swayga" Rate e t g+/PT) - Rate cnhancement = el-sagt/RT) = -lo RNH - this is with a catalyst cset. Cip O O M T o-Pong AND o R Trond Skytte 9 og CH, Cop rx coordinate CATALYTIC MECHANISMS Proteases: enzymes that - Acid-base give & take H+ hydrolyze peptide bonds Covakam dhange reaction path - 4 dasses of proteases - M otal len: redox cutatoris, pku shitters - Eletrostatic : Pretorential lutumctiane w Serine - digestive enzynos tunitim statu Cysteine capses Ceptene tases) tha amino auids m Acid -Buse, Catalusis 4sparty - Hiv protcase Histidine Serine Glutamate Arginine lysteine Aspartate M etalloproteases-bacteria Lysine TyrosineINHIBITORS OVERVIEW comptar waktmte at desite outcome of thhibition is NO DEAMON competitive Inhibition Vs. Incompetitive Tnhibition -Transition - Bind reversibly -Bind reversibly stute arg. - cannot bind sulestrate - Binck Emyme-plex logs & | * can be overcome by ES] * Lan only be partially overcome make good - Inureuses Kupptrent by Es - De reases ku aparent Inhibitors - No effect on Vmax - Decreases Vmes parent -K: CELI - K: LEICS] CEL] Products compctitve v. m d', Vol LEIS7 a' 1.5 plotted as d2. a fx of Sustrate ds4 contato Vnish HHI Sk SKU 1KIK a: 4 ds2 LS Ino inblation) Cno inha A 1 Csa - Taka ( V (si) + k m 4ku kazkoku Skudsku maku lkn sku MIX cd Ihhikortion - Competitive & Unwmpetitive - Vmax Vmax.de Properties - ak a' hot pussarily the same - if they are the same, lines wald Ynteis cet on x-axis - Increase or devrede kurre - Decregses Vmaxpo.by: (activation thers) BIOLHEM I STUDYGUIDE EXAM 3 ENZYMES Enzymes are biological catalysts Emyms are highly - Most chrymes are proteins (some RNA) SPECIFIC: - The rules ot catalysts from Gain Chem - Chiral apply: - only recognize one - Catalysts increase the rate of the Stereoisomer of a Substrate reaction -only product one - Work in the forward & riverse stureoisomer as a directions (2) product - Catalysts Increase the rate of rx - Promls cuity : emymes can bind other substrates selectively this loves -Binding & stabilizing the transition * te a state species of the reaction specfidty vs. selectivity , L - orient (colocalize reactants blinds on one substrate di Llaming ligand - this decreases entropy Letter than the other ch) - The rate of a reaction has - chymotrypsih NO EFFECT on the FREE ENEROTYCG) PL-NER HO** What is an chyma cofactori? - Cotuctor: a substance Lother than the substrate) , whose presence is essential for cmyme i op'tHo3. chysstyper - Needed in many redox reactions R 0 +HDR - Examples: - chymotrysih can hydro- * Metal ions (cun be reduced oxidized) lyric ester bonds, but - organic cosubstrates (redox cupb e) 1000 fines less efficient - NAD /NADH *FADH / FADH2 * CATALYTIC PERFECTION - Prosthetic groups 108 to 10 m's" - Acctylcholinesterase - ATP (GTP cosubstrates - Phosphatte isomerase * Cosubstrates must be regenerated - Cosubstrates may require energy input MAIN DAPORT ERN FORWOLA paprtidei thNR activity CUB

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