ArticleBiochemistry2011
Structural and biochemical characterization of ZhuI aromatase/cyclase from the R1128 polyketide pathway.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 57 citations in OpenAlex.
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- Biosynthesis and Microbial Production of Carminic Acid: From Pathway Elucidation to Synthetic Biology.Microorganisms · 2026Review
- Identification and heterologous expression of an NRPS biosynthetic gene cluster responsible for the production of the pyrazinones Ichizinone A, B and C.Microbial cell factories · 2025Article
- Analysis of the Setomimycin Biosynthetic Gene Cluster fromInternational journal of molecular sciences · 2024Article
- An unusual aromatase/cyclase programs the formation of the phenyldimethylanthrone framework in anthrabenzoxocinones and fasamycin.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Domain swapping of the C-terminal helix promotes the dimerization of a novel ribonuclease protein from Mycobacterium tuberculosis.Protein science : a publication of the Protein Society · 2023Article
- Early Steps in the Biosynthetic Pathway of Rishirilide B.Molecules (Basel, Switzerland) · 2020Article
- Programmable polyketide biosynthesis platform for production of aromatic compounds in yeast.Synthetic and systems biotechnology · 2020Article
- Solution NMR structure of CGL2373, a polyketide cyclase-like protein from Corynebacterium glutamicum.Proteins · 2020Article
- Heterologous production of the widely used natural food colorant carminic acid in Aspergillus nidulans.Scientific reports · 2018Article
- The putative polyketide cyclase MSMEG_0129 from Mycobacterium smegmatis: purification, crystallization and X-ray crystallographic analysis.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Non-enzymatic pyridine ring formation in the biosynthesis of the rubrolone tropolone alkaloids.Nature communications · 2016Article
- Structural and functional analysis of two di-domain aromatase/cyclases from type II polyketide synthases.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Modeling linear and cyclic PKS intermediates through atom replacement.Journal of the American Chemical Society · 2014Article
- A thermoacidophile-specific protein family, DUF3211, functions as a fatty acid carrier with novel binding mode.Journal of bacteriology · 2013Article
- Rational reprogramming of fungal polyketide first-ring cyclization.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Insight into the molecular basis of aromatic polyketide cyclization: crystal structure and in vitro characterization of WhiE-ORFVI.Biochemistry · 2012Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Aromatic polyketides comprise an important class of natural products that possess a wide range of biological activities. The cyclization of the polyketide chain is a critical control point in the biosynthesis of aromatic polyketides. The aromatase/cyclases (ARO/CYCs) are an important component of the type II polyketide synthase (PKS) and help fold the polyketide for regiospecific cyclizations of the first ring and/or aromatization, promoting two commonly observed first-ring cyclization patterns for the bacterial type II PKSs: C7-C12 and C9-C14. We had previously reported the crystal structure and enzymological analyses of the TcmN ARO/CYC, which promotes C9-C14 first-ring cyclization. However, how C7-C12 first-ring cyclization is controlled remains unresolved. In this work, we present the 2.4 Å crystal structure of ZhuI, a C7-C12-specific first-ring ARO/CYC from the type II PKS pathway responsible for the production of the R1128 polyketides. Though ZhuI possesses a helix-grip fold shared by TcmN ARO/CYC, there are substantial differences in overall structure and pocket residue composition that may be important for directing C7-C12 (rather than C9-C14) cyclization. Docking studies and site-directed mutagenesis coupled to an in vitro activity assay demonstrate that ZhuI pocket residues R66, H109, and D146 are important for enzyme function. The ZhuI crystal structure helps visualize the structure and putative dehydratase function of the didomain ARO/CYCs from KR-containing type II PKSs. The sequence-structure-function analysis described for ZhuI elucidates the molecular mechanisms that control C7-C12 first-ring polyketide cyclization and builds a foundation for future endeavors into directing cyclization patterns for engineered biosynthesis of aromatic polyketides.
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