Room 2621 K. Kristoffer Andersson ¡­

Room 2621

K. Kristoffer Andersson Tuesdays 09.15-12.00, Thursdays 09.15-12.00, room 2621 Biologihuset 2nd floor

1-3 Introduction to enzymes in general and steady state kinetics; alcohol dehydrogenase, stereospecific reactions, tunneling, cofactors. One substrate reactions, saturation, Ks, Km, steady state, Vmax, plots. Several different types of simple enzyme inhibition and activation +plots, suicide inhibition. HB 51-106; VV 459-486

4-6. Heme-proteins, myoglobin and hemoglobins, axial ligands, tetra pyrrols. Binding of ligands to protein. Sigmiod kinetics and allosteric enzymes. Hill and Adair equations, models. VV 320-353, HB 5-49

7-9. Reversible reactions, Development and use of Haldane equations. Use of King-Altman technique for net velocity equation. Multi-substrate kinetics, sequential and none sequential enzyme mechanism. VV 481-493, HB 108-130

10-12 Timedependent reactions, transient kinetics and methods, pH effects and Cryobiochemistry HB 139-158, 222-241, VV 281-283, 486-487, Handout

13-15 Physical chemical methods (chromophores, CD, flourence, Raman, resonance Raman, NMR and EPR) and protein structure. VV 219-271 HB 188-222 (DS 61-120, 215-285)

16- 18 Some organic and general mechanisms of enzymes, isotope studies. Radicals, nucleophiles, different intermediates, group transfers, C-C bond reactions, acid-base catalysis, covalent catalysis, RNAse A, proximity and orientation, transition state binding, lysozyme, serin proteases, hexokinase, phospho- glycerate mutase, phosphoglucose isomerase, aldolase, triose phosphate isomerase. VV 496-529, 552-565, 585-600

19- 21 Some enzymes and proteins with cofactors (e.g. metals, NADH, flavin/pterins), phosphoglycerate mutase and kinase, hexokinase, enolase, carbonic anhydrase, carboxypeptidase A, pyruvate decarboxylase, alcohol dehydrogenase, gluceraldehyde-3-phosphate dehydrogenase, glutathione reductase, several different reactions of PLP, urea cycle, carbamyl phosphate, homocysteine, glycine cleavage system, SAM, tetrahydrobiopterin hydroxylases NIH shift), multienzyme complexes (pyruvate dehydrogenase TPP CoA Lipoic acid FAD). VV 600-606, 756-762, 768-781, 985-988, 996-1000, 1007-1013

22- 24 heme synthesis C5-pathway and breakdown, active amines, biotin, THF, glutathione cycle Nitrogenase and nitrogen fixation. Oxidation-reduction and electron transport, some iron-sulfur proteins, aconitase, Xanthine oxidase Mo-pterin, Wo-pterin and MoFe in nitrogenase, Ni and V enzymes, Complex II. VV 571-587, 783-788, 802-812, 1013-1036, 1043-1049, 1094-1096

25-27 Other proteins related to citric acid cycle, cytochrome oxidase structure and mechanism, Complex II+ III, ATPase, O2- chemistry, hydroxylations (P450/MMO), peroxidases and superoxide dismutases, some NO chemistry (e.g., nitrogen oxide synthase, NOS). VV 480-481, 533-534, 671-675, 726-738, 812-834

28-30 Oxidative stress, radical enzymes, ribonucleotide reductase + thioredoxin, Cobalamin (B12) enzymes methylmalonyl CoA mutase and homocysteine methyltransferase, Lipoxygenase, prostaglandine H2 synthase, Photosyntesis light reaction, synthesis of O2 . VV 871-896, 922-927, 1003, 1080 -1088

Books: VV; Voet and Voet Biochemistry third edition (2004) John Wiley & Sons, New York

HB; Hans Bisswanger, Enzyme Kinetics, principles and methods (2002)

+ DS; David Sheehan, Physical Biochemistry book from MBV 4020 course

Reference literature available in the library:

I. H. Segel (1975): Enzyme kinetics

T. Palmer: Understanding enzymes. 4 Edition 1995 (Ellis Horwood Limited, Chichester)

T. Palmer UTDRAG KJB 400 Biokjemi Hovedfag

W.W. Cleland in "The enzymes" 3rd ed., P. Boyer, ed, Vol., pp. 1-65

A. Cornish-Bowden (1995): Fundamentals of enzyme kinetics

Methods in Enzymology: Biochemical Spectroscopy (V. 246), Enzyme kinetics and mechanism (V.249)