Ή-Transaminase from Neosartorya fischeri

<strong>ω-Transaminase from Neosartorya fischeri</strong>_x000D_ <strong>Catalog number:</strong> B2016603_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 5 mg_x000D_ <strong>Molecular Weight or Concentration:</strong> N/A_x000D_ <strong>Supplied as:</strong> Powder_x000D_ <strong>Applications:</strong> a molecular tool for various biochemical applications_x000D_ <strong>Storage:</strong> −20°C_x000D_ <strong>Keywords:</strong> ω-Transaminase, Neosartorya fischeri_x000D_ <strong>Grade:</strong> Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity >18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong> _x000D_ 1: Gao X, Wei P. [Advances in molecular modification of ω-transaminase] Sheng Wu Gong Cheng Xue Bao. 2018 Jul 25;34(7):1057-1068. _x000D_ 2: Zhang Z, Liu Y, Zhao J, Li W, Hu R, Li X, Li A, Wang Y, Ma L. Active-site engineering of ω-transaminase from Ochrobactrum anthropi for preparation of L-2-aminobutyric acid BMC Biotechnol. 2021 Sep 25;21(1):55. _x000D_ 3: Li Z, Liu Y, Luo Q, Lü X. [The advance of ω-transaminase in chiral amine biosynthesis in China from the perspective of patents] Sheng Wu Gong Cheng Xue Bao. 2023 Aug 25;39(8):3169-3187. _x000D_ 4: Ramírez-Palacios C, Wijma HJ, Thallmair S, Marrink SJ, Janssen DB. Computational Prediction of ω-Transaminase Specificity by a Combination of Docking and Molecular Dynamics Simulations J Chem Inf Model. 2021 Nov 22;61(11):5569-5580. _x000D_ 5: Wegner U, Matthes F, von Wirén N, Hajirezaei MR, Bode R, Kunze G, Rauter M. A transaminase with β-activity from Variovorax boronicumulans for the production of enantiopure β-amino acids Heliyon. 2022 Dec 30;9(1):e12729. _x000D_ 6: Chen R, Su K, Zhang Y, Zhu Y, Liu J, Xu J. Co-crystal structure provides insights on transaminase CrmG recognition amino donor L-Arg Biochem Biophys Res Commun. 2023 Oct 1;675:41-45. _x000D_ 7: Yang L, Zhang K, Xu M, Xie Y, Meng X, Wang H, Wei D. Mechanism-Guided Computational Design of ω-Transaminase by Reprograming of High-Energy-Barrier Steps Angew Chem Int Ed Engl. 2022 Dec 23;61(52):e202212555. _x000D_ 8: Meng Q, Ramírez-Palacios C, Capra N, Hooghwinkel ME, Thallmair S, Rozeboom HJ, Thunnissen AWH, Wijma HJ, Marrink SJ, Janssen DB. Computational Redesign of an ω-Transaminase from Pseudomonas jessenii for Asymmetric Synthesis of Enantiopure Bulky Amines ACS Catal. 2021 Sep 3;11(17):10733-10747. _x000D_ 9: Wang C, Tang K, Dai Y, Jia H, Li Y, Gao Z, Wu B. Identification, Characterization, and Site-Specific Mutagenesis of a Thermostable ω-Transaminase from Chloroflexi bacterium ACS Omega. 2021 Jun 25;6(26):17058-17070. _x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/24487538">10: Gustavsson M, Muraleedharan MN, Larsson G. Surface expression of ω-transaminase in Escherichia coli Appl Environ Microbiol. 2014 Apr;80(7):2293-8. </a>_x000D_ <br><strong>Products Related to ω-Transaminase from Neosartorya fischeri can be found at</strong> <a href="https://moleculardepot.com/product-category/Enzymes/"> Enzymes</a>