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B8. Links and References

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    iconexternal_link.gifThe Enzyme Function Initiative is developing such tools to predict in vitro enzymatic and in vivo physiological functions of unknown enzymes.

    iconexternal_link.gifUniprot, a web base resources that hold protein sequence and functional information, has over 44 million protein sequences (derived from nucleotide sequences) and most have no well defined protein function.

    iconexternal_link.gifMetabolic Docker: uses molecular docking as a basis for predicting the function of enzymes. It supports docking both ground state and high energy intermediate forms of metabolites and commercially available compounds to protein structures

    Other Types of Enzymes

    The three enzymes studied above are all hydrolases - enzymes that catalyze the hydrolysis of bonds (either amide or acetal). This is only one class of six different reaction types that have been categorized by the Enzyme Commission of the International Union of Biochemistry and Molecular Biology. The six types (all external links) include:

    EC1: Oxidioreductases - oxdiation/reduction reactions (we will discuss these in Chapter 8B)

    EC2: Transferases - acyl, glycosyl, 1C, N, O, aldehydes, ketones, etc

    EC3: Hydrolases

    EC4: Lyases - cleavage of C-C, C-O, C-N, C-S, etc. bonds

    EC5: Isomerases - racemases, epimerases, cis-trans isomerases

    EC6: Ligases - form C-C, C-O, C-N, etc bonds

    Other Links

    iconexternal_link.gifEnzyme Nomenclature Database: Interactive site to search information on enzymes using EC system of nomenclature.

    iconexternal_link.gifBRENDA: (Brauschweig Enzyme Database) Comprehensive Enzyme Information System

    iconexternal_link.gifKEGG PATHWAY: collection of manually drawn pathway maps representing our knowledge on the molecular interaction and reaction networks using KEGG, Kyoto Encyclopedia of Genes and Genomes

    iconexternal_link.gifFMM (From Metabolite to Metabolite) - reconstructs metabolic pathways from one metabolite to another

    References

    1. Wolan, D. et al. Small-Molecule Activators of a Proenzyme. Science 326, 853 (2009)
    2. Wang, Y. et al. Crystal structure of a rhomboid family intramembrane protease. Nature. 444, 179 (2006)
    3. Freeman, M. Proteolysis within the membrane: rhomboids revealed. Nature Reviews: Molecular Cell Biology. 5, p 188 (2004)
    4. Borman, S. Much ado about enzyme mechanisms. C&EN. pg 35 (Feb 23, 2004)
    5. Garcia-Cioloca, M. Goa, J., Karplus, M. and Truhlar, D. How Enzymes Work: Analysis by modern rate theory and computer simulation Science. 303, pg 186 (2004)
    6. Benkovic, St. & Hammes-Schiffer, S. A Perspective on Enzyme Catalysis. Science. 301, pg 1196 (2003)
    7. Takasugi, N. et al. The role of presenilin cofactors in the γ-secretase complex. Nature. 422, pg 438 (2003)
    8. Weihofen et al. Identification of Signal Peptide Peptidase, a Presenilin-Type Aspartic Protease. Science, 296, pp. 2156, 2215,
    9. Vocadlo. D. et al. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature. 412. pg 835 (2001)
    10. Walsh, C. Enabling the Chemistry of Life. Great review article on enzymes mechanisms. Nature. 409, pg 226 (2001)
    11. Koeller and Wong. Enzymes for Chemical Synthesis. Nature 409. pg 232 (2001)
    12. Simeonov et al. Blue-Fluorescent Antibodies. Science. 290, pg 286, 307 (2000)
    13. Huntington et al. Structure of a serpin-protease complex shows inhibition by deformation. Nature. 407, pg 923 (2000)
    14. New Way to Study Closely related proteins (remodeling proteins to make them more susceptible to inhibition) Science 289. pg 2029 (2000)
    15. Vocadlo et al. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature. 412. pg 835 (2001)
    16. Istan and Deisenhofer. Structural Mechanism for Statin Inhibition of HMG-CoA Reductase. Science. 292, pg 1160 (2001)
    17. Heine et al. Observations of Covalent Intermediates in an Enzyme Mechanism at Atomic Resolution. Science 294. pg 369 (2001)
    18. Carpenter et al. Structure of dehydorquinate synthase reveals an active site capable of multi-step catalysis. Nature. 394, pg 299 (1998)
    19. Kohen et al. Tunnel Vision (on why activity of therophilic enzymes (>60oC) is low or absent at mesophilic temperatures (< 40oC) - from reduction of flexibility of thermophilic enzymes at mesophilic temperatures - quantum tunneling explanation). Nature. 399, pg 417, 496 (1999)
    20. Finnin et al. Structure of a histone deacetylase homologue bound to the TSA and SAHA inhibitors (and mechanism). Nature. pg 189, September 1999.
    21. Ondrechen. THEMATICS: A simple computational predictor of enzyme function from structure. Proc. Natl. Acad. Sci. USA, 98, pg 12473 (2001 )

    This page titled B8. Links and References is shared under a CC BY-NC-SA license and was authored, remixed, and/or curated by Henry Jakubowski.

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