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  Molecular basis of Celmer's rules: Stereochemistry of catalysis by isolated ketoreductase domains from modular polyketide synthases

Siskos, A. P., Baerga-Ortiz, A., Bali, S., Stein, V., Mamdani, H., Spiteller, D., et al. (2005). Molecular basis of Celmer's rules: Stereochemistry of catalysis by isolated ketoreductase domains from modular polyketide synthases. Chemistry and Biology, 12(10), 1145-1153.

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 Creators:
Siskos, A. P., Author
Baerga-Ortiz, A., Author
Bali, S., Author
Stein, V., Author
Mamdani, H., Author
Spiteller, D.1, Author           
Popovic, B., Author
Spencer, J. B., Author
Staunton, J., Author
Weissman, K. J., Author
Leadlay, P. F., Author
Affiliations:
1Department of Bioorganic Chemistry, MPI for Chemical Ecology, Max Planck Society, ou_24028              

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Free keywords: Fatty-acid synthase Erythromycin biosynthesis Chain extension 4-pro-s hydride Mechanism Binding Construction Antibiotics Specificity Expression Biochemistry & Biophysics in Current Contents(R)/Life Sciences
 Abstract: A system is reported for the recombinant expression of individual ketoreductase (KR) domains from modular polyketide synthases (PKSs) and scrutiny of their intrinsic specificity and stereospecificity toward surrogate diketide substrates. The eryKR(1) an

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 Dates: 2005
 Publication Status: Issued
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 Identifiers: Other: BOL379
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Title: Chemistry and Biology
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Source Genre: Journal
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Pages: - Volume / Issue: 12 (10) Sequence Number: - Start / End Page: 1145 - 1153 Identifier: -