Abstract
AlpK is an essential monooxygenase involved in the biosynthesis of kinamycin. It catalyzes the C5-hyfroxylattion of the crucial benzo[b]-fluorence intermediate in kinamycin synthesis. However, the structure and mechanism of AlpK is unclear. Here, we report the first structure of AlpK in complex with FAD. Our structure sheds light on the catalytic mechanism of AlpK.
Keywords:
AlpK; Crystal structure; Kinamycin.
Copyright © 2019 Elsevier Inc. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / chemistry*
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Bacterial Proteins / metabolism
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Crystallography, X-Ray
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Mixed Function Oxygenases / chemistry*
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Mixed Function Oxygenases / metabolism
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Models, Molecular
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Protein Conformation
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Protein Multimerization
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Quinones / metabolism
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Sequence Alignment
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Streptomyces / chemistry
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Streptomyces / enzymology*
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Streptomyces / metabolism
Substances
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Bacterial Proteins
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Quinones
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kinamycin A
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Mixed Function Oxygenases