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Research Groups (1)

Research Groups (1)

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Published by Suji Pranav

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Published by: Suji Pranav on Feb 22, 2012
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1)
 
Professor Peter Leadlay FRS FRSC
http://www.bio.cam.ac.uk/~pflgroup/publications.htmhttp://www.bio.cam.ac.uk/~pflgroup/index.html
Herchel Smith Professor of Biochemistry,Department of Biochemistry,University of Cambridge.
T
elephone: (01223) 333656Fax: (01223) 766002pfl10@mole.bio.cam.ac.ukDepartmental Web PageBiotica
T
echnology Ltd.
 
(170
publications)
Wilkinson, B., Foster, G., Rudd, B. A.,
T
aylor, N. L., Blackaby, A. P., Sidebottom, P. J.,Cooper, D. J., Dawson, M. J., Buss, A. D., Gaisser, S., Bohm, I. U., Rowe, C. J., Cortés, J.,Leadlay, P. F. & Staunton, J. (2000).Novel octaketide macrolides related to 6-deoxyerythronolide B provide evidence for iterative operation of the erythromycin polyketidesynthase.
Chemistry & Biology,
7
, 111-7.
y
 
Leadlay P.F., Staunton J., Oliynyk M., Bisang C., Cortes J., Frost E., Hughes-
T
homas Z.A.,Jones M.A., Kendrew S.G., Lester J.B., Long P.F., McArthur H.A., McCormick E.L., OliynykZ., Stark C.B., Wilkinson C.J. (2001).Engineering of complex polyketide biosynthesis--insights from sequencing of the monensin biosynthetic gene cluster.
 J.
Ind 
.
Microbiol 
.
 Biotechnol 
.
 ,
 
6
, 360-7. Review.Lowden P.A., Wilkinson B., Bohm G.A., Handa S., Floss H.G., Leadlay P.F., Staunton J.(2001).Origin and
T
rue Nature of the Starter Unit for the Rapamycin Polyketide Synthase.
 A
ngewandte Chemie International Edition
.
,
40
, 777-779Gaisser, S., Kellenberger, J.L., Kaja, A.L., Weston, A.J., Lill, R.E., Wirtz, G., Kendrew, S.G.,Low, L., Sheridan, R.M., Wilkinson, B., Galloway, I.S., Stutzman-Engwall, K., McArthur,H.A.I., Staunton, J. and
Leadlay, P.F.
(2003).Direct production of ivermectin-like drugsafter domain exchange in the avermectin polyketide synthase of 
S
treptomyces avermitilis
 A
T
CC31272.
Org
.
Biomol 
.
Chem
.
,
1
, 2840-2847
 
2
)
 
Dr. Adrian Keatinge-Clay
Assistant Professor The University of Texas at AustinDepartment of Chemistry and BiochemistryAustin, TX 78712-1167Office: WEL 4.230BOffice Phone: (512) 471-2977E-mail:adriankc@mail.utexas.edu Lab: WEL 4.234Lab Phone: (512) 471-3156
P
ublications lin
k:http://keatinge-clay.cm.utexas.edu/research/publications.html
Many important pharmaceuticals, including the antibiotic erythromycin and theimmunosuppressant rapamycin, belong to a diverse class of molecules called polyketides. Thesecomplex molecules are synthesized by modular polyketide synthases (PKSs) - enormousenzymes that are directly analogous to assembly lines. Our group seeks to understand thischemical machinery and engineer it to produce new molecules and new medicines.
Biosynthesis
Each enzyme within these megasynthases operates on a polyketide only once during itssynthesis. Transformations catalyzed by PKS enzymes include carbon-carbon bond formation,cyclizations, and stereospecific reductions and eliminations. Our research attempts to determinethe mechanisms and specificities of each enzyme type in order to genetically engineer PKSs tomake both derivatives of known polyketides and libraries of completely novel polyketides.
Biophysics
The domain boundaries of enzymes within PKSs have recently been identified, enablingstructural studies of isolated domains. The atomic resolution structures of PKS enzymes help build a description of the overall PKS assembly line architecture. They also help elucidate whatinteractions between PKS enzymes and their substrates are required for correct polyketide processing. The structures of several key PKS enzymes remain to be determined.
Biocatalysis
PKSs are the enzymatic champions of organic synthesis, performing complex, stereocontrolledreactions on diverse carbon chains. Our lab is learning how to harness the catalytic potential of isolated PKS enzymes and utilize them to perform desirable chemical transformations. As PKS biocatalysts are catalytically active under ambient conditions in an aqueous environment, theycan be considered a new paradigm in "green chemistry."
 
3
)Chaitan Khosla http://www.stanford.edu/dept/chemistry/faculty/khosla/
Title:
Chair, Chemical Engineering; Wells H. Rauser and HaroldM. Petiprin Professor in the School of Engineering; Professor of Chemical Engineering, Chemistry, and Biochemistry, by courtesy(b. 1964)
Education:
B.Tech., 1985, Indian Institute of Technology;Ph.D.,1990, California Institute of Technology; Postdoctoral,John Innes Centre, U.K., 1990-91
Awards:
Dreyfus New Investigator Award, 1991; NSF YoungInvestigator Award, 1994-99; Packard Fellowship for Scienceand Engineering, 1994-99; AIChE Allan P. Colburn Award,1997; ACS Lilly Award in Biological Chemistry, 1999; NSFAlan T. Waterman Award, 1999; ACS Pure Chemistry Award,2000; Caltech Distinguished Alumni Award, 2000; Member,American Academy of Arts and Sciences, 2007; Arthur C. CopeScholar Award, 2009; Member, National Academy of Engineering, 2009
Research Area:
Bioorganic and Biophysical Chemistry
P
hone:
650-723-6538
E-mail:
 khosla@stanford.edu 
Website:
 The Khosla Group 
P
rincipal Research Interests
Research interests in this laboratory lie at the interface of chemistry and medicine.For the past several years, we have investigated the catalytic mechanisms of modular megasynthases such as polyketide synthases, with the concomitant goal of harnessing their  programmable chemistry for preparing pharmaceutically relevant natural products. Recentaccomplishments include methods for heterologous production of polyketides; geneticallyreprogrammed biosynthesis of anthraquinones and polypropionates; and chemo-biosynthesis of new polyketides not readily affordable by synthetic or biological methods alone. Thesemethodologies are already finding practical use. At the same time, we have placed a major emphasis on the biochemistry and structural biology of these giant protein assemblies.Fundamental insights into assembly line biosynthetic mechanisms have emerged, including thefinding that protein-protein interactions play a central role in intermodular communications. Inturn, these insights are highlighting opportunities for enhancing the efficiency of biosyntheticengineering. Over the next decade we envision that the predictive power of polyketide biosynthetic engineering will mature analogous to current protein engineering capabilities.

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