Detail of "1264-57-9"

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Preparation of N-acylated proteins modified with fatty acids having a specific chain length using an insect cell-free protein synthesis system

All Rights Reserved. Preparation of N-acylated proteins modified with fatty acids having a specific chain length using an insect cell-free protein synthesis system. Suzuki, Takashi; Ito, Masaaki; Ezure, Toru; Shikata, Masamitsu; Ando, Eiji; Utsumi, Toshihiko; Tsunasawa, Susumu; Nishimura, Osamu (Life Science Laboratory, Analytical and Measuring Instruments Division, Shimadzu Corporation, Kyoto 604-8511, Japan). Bioscience, Biotechnology, and Biochemistry, 71(1), 261-264 (English) 2007 Japan Society for Bioscience, Biotechnology, and Agrochemistry. CODEN: BBBIEJ. ISSN: 0916-8451. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Section cross-reference(s): 9 To establish a strategy to generate N-acylated proteins modified with fatty acids having a specific chain length, tGelsolin-streptag, an epitope-tagged model protein having an N-myristoylation motif, was synthesized using an insect cell-free protein synthesis system in the presence of acyl-CoA with various fatty acid chain lengths. It was found that the fatty acid species attached to the N-termini fully depended on the acyl-CoA species added to the reaction mixt.In this experiment, several chemicals are used like 1264-57-9 and 362-66-3 N-Acylated proteins with fatty acid chain lengths of 8, 10, 12, and 14 were generated successfully. .

Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase

All Rights Reserved. Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase. Crawford, Jason M.; Dancy, Blair C. R.; Hill, Eric A.; Udwary, Daniel W.Chemicals with cas numbers 1264-57-9 and 867-81-2 also play role.; Townsend, Craig A. (Dep. Chem., The Johns Hopkins Univ., Baltimore, MD 21218, USA). Proceedings of the National Academy of Sciences of the United States of America, 103(45), 16728-16733 (English) 2006 National Academy of Sciences. CODEN: PNASA6. ISSN: 0027-8424. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Polyketides are a class of natural products that exhibit a wide range of functional and structural diversity. They include antibiotics, immunosuppressants, antifungals, antihypercholesterolemics, and cytotoxins. Polyketide synthases (PKSs) use chem. similar to fatty acid synthases (FASs), although building block variation and differing extents of redn. of the growing polyketide chain underlie their biosynthetic versatility. In contrast to the well studied sequential modular type I PKSs, less is known about how the iterative type I PKSs carry out and control chain initiation, elongation, folding, and cyclization during polyketide processing. Domain structure anal. of a group of related fungal, nonreducing PKSs has revealed well defined N-terminal domains longer than commonly seen for FASs and modular PKSs. Predicted structure of this domain disclosed a region similar to malonyl-CoA:acyl-carrier protein (ACP) transacylases (MATs). MATs play a key role transferring precursor CoA thioesters from soln. onto FASs and PKSs for chain elongation. On the basis of site-directed mutagenesis, radiolabeling, and kinetics expts. carried out with individual domains of the norsolorinic acid PKS, we propose that the N-terminal domain is a starter unit:ACP transacylase (SAT domain) that selects a C6 fatty acid from a dedicated yeast-like FAS and transfers this unit onto the PKS ACP, leading to the prodn. of the aflatoxin precursor, norsolorinic acid. These findings could indicate a much broader role for SAT domains in starter unit selection among nonreducing iterative, fungal PKSs, and they provide a biochem. rationale for the classical acetyl "starter unit effect.". .