Enzimologija
Nastavnik:
Tanja Ćirković Veličković
Pregled
Opšte informacie o predmetu i načinu ocenjivanja
Literatura
Opšti pojmovi
Nomenklatura enzima
Uvodna znanja
Program i organizacija vežbi
Teorijske vezbe – izračunavanja u enzimologiji
Laboratorijske vežbe: osnovna odredjivanja u enzimologiji
Laboratorijske vežbe: Razni aspekti primene enzima
Fond časova predavanja i vežbi: 3 + 3 (teorijske vežbe)
Asistent: Marija Stojadinovic i Dragana Stanic
Način ocenjivanja
Predavanja: 10 bodova
Kolokvijum 1: 20 bodova
Kolokvijum 2: 20 bodova
Seminarski rad: 5 bodova
Problemski zadatak: 20 bodova
Usmeni deo ispita: 25 bodova
Literatura
Structure and mechanism in protein science, Alan Fersht
Enzimologija: Laboratorijski priručnik, Radivoje Prodanović i Tanja Ćirković Veličković
Zbirka zadataka iz enzimologije, Ivanka Karadžić
Enzyme catalysis, not different, just better!
Katalizator je supstanca koja dovodi do ubrzanja hemijske reakcije, tako da se pri tom promena G ne menja (IUPAC, 1981.)
Biološki katalizatori:
Proteini (enzimi, abzimi)
RNK (ribozimi)
Mimetici enzima
- Šta enzim radi?
Struktura proteina – enzima
Hemijska kinetika – enzimska kinetika
Sukcinat dehidrogenaza sa vezanim hemom (prostetičnom grupom)
Enzim
Monomeran
Homo/hetero dimeran, trimeran etc
Oligomeran
Multienzimski kompleksi


Holoenzim (apoenzim + kofaktor/koenzim)
Kofaktor
Koenzim
Prosteticna grupa (čvrsto vezan kofaktor)
Nomenklatura
Trivijalna imena enzima
E.C. nomenklatura
E.C. Nomenklatura enzima
Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes by the Reactions they Catalyse
http://www.chem.qmul.ac.uk/iubmb/enzyme/
EC 1.1 Oksidoreduktaze
Acting on the CH-OH group of donors
Contents EC 1.1.1 With NAD or NADP as acceptor
EC 1.1.2 With a cytochrome as acceptor
EC 1.1.3 With oxygen as acceptor
EC 1.1.4 With a disulfide as acceptor
EC 1.1.5 With a quinone or similar compound as acceptor
EC 1.1.99 With other acceptors

EC 2 Transferaze
EC 3 Hidrolaze
EC 4 Liaze
EC 5 Izomeraze
EC 6 Ligaze
EC 1 Oxidoreductases 
 
EC 1.1Acting on the CH-OH group of donors
EC 1.2Acting on the aldehyde or oxo group of donors
EC 1.3Acting on the CH-CH group of donors
EC 1.4Acting on the CH-NH2 group of donors
EC 1.5Acting on the CH-NH group of donors
EC 1.6Acting on NADH or NADPH
EC 1.7Acting on other nitrogenous compounds as donors
EC 1.8Acting on a sulfur group of donors
EC 1.9Acting on a heme group of donors
EC 1.10Acting on diphenols and related substances as donors
EC 1.11Acting on a peroxide as acceptor
EC 1.12Acting on hydrogen as donor
EC 1.13Acting on single donors with incorporation of molecular oxygen (oxygenases)
EC 1.14Acting on paired donors, with incorporation or reduction of molecular oxygen
EC 1.15Acting on superoxide radicals as acceptor
EC 1.16Oxidising metal ions
EC 1.17Acting on CH or CH2 groups
EC 1.18Acting on iron-sulfur proteins as donors
EC 1.19Acting on reduced flavodoxin as donor
EC 1.20Acting on phosphorus or arsenic in donors
EC 1.21Acting on X-H and Y-H to form an X-Y bond
EC 1.97Other oxidoreductases
E.C. vs. Trivijalna nomenklatura
EC 1.1.1.1 alcohol dehydrogenaseEC 1.1.1.2 alcohol dehydrogenase (NADP+)EC 1.1.1.3 homoserine dehydrogenaseEC 1.1.1.4 (R,R)-butanediol dehydrogenaseEC 1.1.1.5 acetoin dehydrogenaseEC 1.1.1.6 glycerol dehydrogenaseEC 1.1.1.7 propanediol-phosphate dehydrogenaseEC 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+)EC 1.1.1.9 D-xylulose reductaseEC 1.1.1.10 L-xylulose reductase
http://www.chem.qmul.ac.uk/iubmb/enzyme/search.html


Searching the Enzyme list
This search form looks at IUBMB Enzyme Nomenclature with a URL starting http://www.chem.qmul.ac.uk/iubmb/enzyme/ All recommended Enzymes are listed on the web. This search excludes other biochemical recommendations on enzyme kinetics, biochemical thermodynamics, and recommendations made by IUBMB only. To search these click here or for more chemical recommendations and other IUPAC recommendations click here.
Search: PEPSIN
Some search terms cause problems:For (S)-stylopine use stylopine otherwise all references with S as an initial are included. For germacrene A use "germacrene A"
 Web Results 1 - 10 of about 32 for pepsin [definition]. (0.06 seconds) 
EC 3.4.23
EC 3.4.23. Aspartic endopeptidases. Contents. EC 3.4.23.1 pepsin A EC 3.4.23.2 pepsin B EC 3.4.23.3 gastricsin EC 3.4.23.4 chymosin EC 3.4.23.5 cathepsin D ...www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/23/ - 5k - Cached - Similar pages
EC 3.4.23.1
Human pepsin A occurs in five molecular forms. Pig pepsin D [1,2] is ... Lee, D. and Ryle, A.P. Pepsin D. A minor component of commercial pepsin ...www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/23/1.html - 5k - Cached - Similar pages
EC 3.4.23.18
In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6 ... proteinase of Aspergillus awamori - an analog of penicillopepsin and pepsin. ...www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/23/18.html - 7k - Cached - Similar pages
EC 3.4.23.3
Other names: pepsin C; pig parapepsin II; parapepsin II ... In peptidase family A1 (pepsin A family). Formerly EC 3.4.4.22. Links to other databases: BRENDA ...www.chem.qmul.ac.uk/iubmb/enzyme/EC3/4/23/3.html - 4k - Cached - Similar pages

IUBMB Enzyme Nomenclature
EC 3.4.23.1
Accepted name: pepsin A
Reaction: Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe1 Val, Gln4 His, Glu13 Ala, Ala14 Leu, Leu15 Tyr, Tyr16 Leu, Gly23 Phe, Phe24 Phe and Phe25 Tyr bonds in the B chain of insulin
Other names: pepsin; lactated pepsin; pepsin fortior; fundus-pepsin; elixir lactate of pepsin; P I; lactated pepsin elixir; P II; pepsin R; pepsin D
Comments: The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis. Human pepsin A occurs in five molecular forms. Pig pepsin D [1,2] is unphosphorylated pepsin A. Type example of peptidase family A1. Formerly EC 3.4.4.1
Links to other databases: BRENDA, EXPASY, GTD, MEROPS, PDB, CAS registry number: 9001-75-6




References:
1. Lee, D. and Ryle, A.P. Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa. Biochem. J. 104 (1967) 735-741. [PMID: 4167464]
2. Lee, D. and Ryle, A.P. Pepsin D. A minor component of commercial pepsin preparations. Biochem. J. 104 (1967) 742-748. [PMID: 4860638]
3. Foltmann, R. Gastric proteinases -structure, function, evolution and mechanism of action. Essays Biochem. 17 (1981) 52-84. [PMID: 6795036]
4. James, M.N.G. and Sielecki, A.R. Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution. Nature 319 (1986) 33-38. [PMID: 3941737]
5. Fruton, J.S. Aspartyl proteinases. In New Comprehensive Biochemistry Vol. 16, Hydrolytic Enzymes (Neuberger, A. and Brocklehurst, K., eds), pp. 1-38 (1987) Elsevier, Amsterdam
6. Tang, J. and Wong, R.N.S. Evolution in the structure and function of aspartic proteases. J. Cell. Biochem. 33 (1987) 53-63. [PMID: 3546346]
7. Pohl, J. and Dunn, B.M. Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site. Biochemistry 27 (1988) 4827-4834. [PMID: 3139029]
acetyl-L-phenylalanyl-L-diiodotyrosine+H2O =acetyl-L-phenylalanine+L-diiodotyrosine
PDB: x-ray struktura pepsina u kompleksu sa inhibitorom
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