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Ing glyoxalase I ning tau. Adua lang ion ning zinc deng kailangan ba neng a-catalyze ning enzyme ing reaction anti ing makalto kareng mangabilug a kule ubi. Makalto ya anting space-filling model ing metung a enzyme inhibitor a ausan dang S-hexylglutathione, a sasapak/kakatmu kareng aduang active site.

Deng enzymes biomolecule lang mag-catalyze (magpabilis) kareng chemical reaction.[1][2] Alus protina la ngan deng enzyme. Kareng reaksion da reng enzyme, ausan dong substrates deng molecule king umpisa ning prosesu. Potang kai, alilan no ning enzyme ba lang maging aliwang molecule, deng produktu. Mangailangan lang enzyme deng halus eganaganang prosesu king metung a cell bang mitaglus king kailaingan a bilis o salusu. Uling eksaktu lang mamiling substrate deng enzyme, at ditak la mu deng papabilisan dang reaksion ibat kareng dakal a pipamilinan, ing kabilugan da reng enzyme king metung a cell ing tutuldu nung sanung metabolic pathway ing mararapat king metung a cell.

Anti reng eganaganang catalyst, gagana la reng enzyme kapamilatan ning pamagbaba king activation energy (Ea or ΔG) ning reaction, ania bigla yang mitatas ing salusu ning reaction. Miliun lang besis/ukdung mas matas deng salusu da ring enzyme reaction kesa kareng katumbas a reaction a e me-catalyze. Kalupa da reng aliwang catalyst, e la magigisan deng enzyme kareng reaction a karelang ka-catalyze, at e ra alilan ing equilibrium da reng reaction a reti. Nanupata, ing pamialiwa da reng enzyme kareng aliwang catalyst, misna lang eksaktu o partikular deti. Sasabian dang apat lang libung 4,000 biochemical reaction deng ka-catalyze da reng enzyme.[3] Ating ditak a RNA molecule, a ausan dang ribozyme, a mag-catalyze kareng reaction, at metung yang maulagang alimbawa ing mapilang dake ning ribosome.[4][5] Magpalto la muring catalysis a kalupa da reng enzyme deng pikudta o artipisial a molecule, a ausan dang artificial enzyme.[6]

Mayayapektuan kareng aliwang molecule ing aktibidad da reng enzyme. Deng inhibitors molecule lang magpasikan king aktibidad. Enzyme inhibitor la reng dakal a panulu ampong lasun. Miyayapektuan murin ing aktibidad kareng temperatura, paligid a kemikal (chemical environment, alimbawa ing pH), ampo ing tapang o konsentrasiun ning substrate. Gagamitan do king industria deng aliwang enzyme, alimbawa king king pamaglalang kareng antibiotic. Bukud kaniti, gagamit lang enzyme deng aliwang produktung gagamitan king bale (al., gagamitan do reng enzyme kareng biological washing powder a paglasong mantsang protina o taba kareng imalan; enzyme kareng pampalambut karni, bang mas malaguang langutan ing karni).

Lon la murin deti

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Dalerayan

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  1. Smith AD (Ed) et al. (1997) Oxford Dictionary of Biochemistry and Molecular Biology Oxford University Press. ISBN 0-19-854768-4
  2. Garrett RH, Grisham CM. (1999) Biochemistry, Second Edition Saunders College Publishing. 426-427. ISBN 0-03-022318-0
  3. Bairoch A. (2000). "The ENZYME database in 2000". Nucleic Acids Res 28: 304-305. doi:10.1093/nar/28.1.304. PMID 10592255. Archived from the original. You must specify the date the archive was made using the |archivedate= parameter. http://www.expasy.org/NAR/enz00.pdf. 
  4. Lilley D (2005). "Structure, folding and mechanisms of ribozymes". Curr Opin Struct Biol 15 (3): 313-23. doi:10.1016/j.sbi.2005.05.002. PMID 15919196. 
  5. Cech T (2000). "Structural biology. The ribosome is a ribozyme". Science 289 (5481): 878-9. doi:10.1126/science.289.5481.878. PMID 10960319. 
  6. Groves JT (1997). "Artificial enzymes. The importance of being selective". Nature 389 (6649): 329-30. doi:10.1038/38602. PMID 9311771. 

Karagdagang babasan

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Etymology and history

Enzyme structure and mechanism

  • Fersht, A. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding. W. H. Freeman, 1998 ISBN 0-7167-3268-8
  • Walsh, C., Enzymatic Reaction Mechanisms. W. H. Freeman and Company. 1979. ISBN 0-7167-0070-0
  • Page, M. I., and Williams, A. (Eds.), 1987. Enzyme Mechanisms. Royal Society of Chemistry. ISBN 0-85186-947-5
  • Bugg, T. Introduction to Enzyme and Coenzyme Chemistry, 2004, Blackwell Publishing Limited; 2nd edition. ISBN 1-4051-1452-5
  • Warshel, A., Computer Modeling of Chemical Reactions in enzymes and Solutions John Wiley & Sons Inc. 1991. ISBN 0-471-18440-3

Thermodynamics

Kinetics and inhibition

  • Athel Cornish-Bowden, Fundamentals of Enzyme Kinetics. (3rd edition), Portland Press (2004), ISBN 1-85578-158-1.
  • Irwin H. Segel, Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems. Wiley-Interscience; New Ed edition (1993), ISBN 0-471-30309-7.
  • John W. Baynes, Medical Biochemistry, Elsevier-Mosby; 2th Edition (2005), ISBN 0-7234-3341-0, p. 57.

Function and control of enzymes in the cell

  • Price, N. and Stevens, L., Fundamentals of Enzymology: Cell and Molecular Biology of Catalytic Proteins Oxford University Press, (1999), ISBN 0-19-850229-X
  • Nutritional and Metabolic Diseases Chapter of the on-line textbook "Introduction to Genes and Disease" from the NCBI.

Enzyme-naming conventions

  • Enzyme Nomenclature, Recommendations for enzyme names from the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.
  • Koshland D. The Enzymes, v. I, ch. 7, Acad. Press, New York, (1959)

Industrial applications

Suglung palual

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