Jianting Zheng
Affiliations: | Chinese Academy of Sciences, Beijing, China |
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Publications
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Wei J, Zhang X, Zhou Y, et al. (2022) Endowing homodimeric carbamoyltransferase GdmN with iterative functions through structural characterization and mechanistic studies. Nature Communications. 13: 6617 |
Saeed AU, Rahman MU, Chen HF, et al. (2022) Structural Insight of KSIII (β-Ketoacyl-ACP Synthase)-like Acyltransferase ChlB3 in the Biosynthesis of Chlorothricin. Molecules (Basel, Switzerland). 27 |
Feng Y, Yang X, Ji H, et al. (2022) The Streptomyces viridochromogenes product template domain represents an evolutionary intermediate between dehydratase and aldol cyclase of type I polyketide synthases. Communications Biology. 5: 508 |
Ali I, Khan A, Fa Z, et al. (2022) Crystal structure of Acetyl-CoA carboxylase (AccB) from Streptomyces antibioticus and insights into the substrate-binding through in silico mutagenesis and biophysical investigations. Computers in Biology and Medicine. 145: 105439 |
Guo Y, Li DF, Zheng J, et al. (2021) Single-component and two-component -nitrophenol monooxygenases: structural basis for their catalytic difference. Applied and Environmental Microbiology. AEM0117121 |
Guo Y, Li DF, Ji H, et al. (2020) Structural and biochemical insights into the substrate selectivity and catalysis of hexachlorobenzene monooxygenase. Applied and Environmental Microbiology |
Zhang F, Ji H, Ali I, et al. (2019) Structural and Biochemical insights to the Recruitment of Acyl Carrier Protein-linked Extender Units in Ansamitocin Biosynthesis. Chembiochem : a European Journal of Chemical Biology |
Zhang F, Shi T, Ji H, et al. (2019) Structural Insights into Substrate Specificity of Acyltransferases from Salinomycin Polyketide Synthase. Biochemistry |
Wang L, Yuan M, Zheng J. (2019) Crystal structure of the condensation domain from lovastatin polyketide synthase. Synthetic and Systems Biotechnology. 4: 10-15 |
He B, Zhou T, Bu X, et al. (2019) Enzymatic Pyran Formation Involved in Xiamenmycin Biosynthesis Acs Catalysis. 9: 5391-5399 |