Papers
2024
[68] One-pot production of vanillin from capsaicinoids through a retrosynthetic enzyme cascade, Advanced Synthesis & Catalysis
Hong-Gon Kim, Youngho Jang and Jong-Shik Shin, https://doi.org/10.1002/adsc.202301454
[67] Reprogramming biocatalytic futile cycles through computational engineering of stereochemical promiscuity to create an amine racemase, Nature Communications
Sang-Woo Han, Youngho Jang, Jihyun Kook, Jeesu Jang, and Jong-Shik Shin, https://doi.org/10.1038/s41467-023-44218-7.
2022
[66] Aromatic L-amino acid decarboxylases : mechanistic features and microbial applications, Applied Microbiology and Biotechnology
Sang-Woo Han, and Jong-Shik Shin, https://doi.org/10.1007/s00253-022-12028-4
[65] One-pot biosynthesis of aromatic D-amino acids and neuroactive monoamines via enantioselective decarboxylation under in situ product removal using ion exchange resin, Biochemical Engineering Journal
Sang-Woo Han, Ye-Ri Choi, Youngho Jang, Jun-Sung Kim, and Jong-Shik Shin, https://doi.org/10.1016/j.bej.2022.108466
2021
[64] Biocatalytic Decarboxylation of Aromatic L-Amino Acids with in situ Removal of Both Products for Enhanced Production of Biogenic Amines, Catalysis Letters
Sang-Woo Han, Ye-Ri Choi, and Jong-Shik Shin, https://doi.org/10.1007/s10562-021-03535-6
[63] Biochemical characterization and synthetic application of aromatic L-amino acid decarboxylase from Bacillus atrophaeus, Applied Microbiology and Biotechnology
Yeri Choi, Sang-Woo Han, Jun-Sung Kim, Youngho Jang, and Jong-Shik Shin, https://doi.org/10.1007/s00253-021-11122-3
2020
[62] The catalytic role of RuBisCO for in situ CO2 recycling in Escherichia coli, Frontiers in Bioengineering and Biotechnology
Ju-Jiun Pang , Jong-Shik Shin, and Si-Yu Li. https://doi: 10.3389/fbioe.2020.543807
[61] In situ removal of inhibitory products with ion exchange resins for enhanced synthesis of chiral amines using ω-transaminase, Biochemical Engineering Journal
Han, Sang-Woo, and Shin Jong-Shik. https://doi.org/10.1016/j.bej.2020.107718
[60] Kinetic Analysis of R-Selective ω-Transaminases for Determination of Intrinsic Kinetic Parameters and Computational Modeling of Kinetic Resolution of Chiral Amine, Applied Biochemistry and Biotechnology
Han, Sang-Woo, and Jong-Shik Shin. https://doi.org/10.1007/s12010-020-03240-x
2019
[59] Conversion of D-Fructose to 5-Acetoxymethyl-2-Furfural Using Immobilized Lipase and Cation Exchange Resin, Molecules
Huynh, Nhan Thanh Thien, Kyung Won Lee, Jin Ku Cho, Yong Jin Kim, Se Won Bae, Jong Shik Shin, and Seunghan Shin. https://doi.org/10.3390/molecules24244623
[58] Rapid and Quantitative Profiling of Substrate Specificity of ω-Transaminases for Ketones, ChemCatChem
Han, Sang-Woo, Youngho Jang, and Jong-Shik Shin. https://doi.org/10.1002/cctc.201900399
[57] In Vitro and In Vivo One-Pot Deracemization of Chiral Amines by Reaction Pathway Control of Enantiocomplementary ω-Transaminases, ACS Catalysis
Han, Sang-Woo, Youngho Jang, and Jong-Shik Shin. https://doi.org/10.1021/acscatal.9b01546
[56] Combinatorial Mutation Analysis of ω‐Transaminase to Create an Engineered Variant Capable of Asymmetric Amination of Isobutyrophenone, Advanced Synthesis & Catalysis
Hong‐Gon Kim Sang‐Woo Han, and Jong‐Shik Shin. https://doi.org/10.1002/adsc.201900184
[55] Activity Improvements of an Engineered ω-Transaminase for Ketones Are Positively Correlated with Those for Cognate Amines, Biotechnology and Bioprocess Engineering
Han, Sang-Woo, and Jong-Shik Shin. https://doi.org/10.1007/s12257-018-0377-3
2018
[54] Base-Free Oxidation of 5-Hydroxymethyl-2-Furfural to 2,5-Furan Dicarboxylic Acid over Basic Metal Oxide-Supported Ruthenium Catalysts under Aqueous Conditions, Journal of Chemical Sciences
Antonyraj, Churchil Angel, Nhan Thanh Thien Huynh, Kyung Won Lee, Yong Jin Kim, Seunghan Shin, Jong Shik Shin, and Jin Ku Cho. https://doi.org/10.1007/s12039-018-1551-z
[53] One-Pot Preparation of d-Amino Acids Through Biocatalytic Deracemization Using Alanine Dehydrogenase and ω-Transaminase, Catalysis Letters
Han, Sang-Woo, and Jong-Shik Shin. https://doi.org/10.1007/s10562-018-2565-3
2017
[52] Active Site Engineering of ω-Transaminase Guided by Docking Orientation Analysis and Virtual Activity Screening, ACS Catalysis
Han, Sang-Woo, Juyeon Kim, Hyun-Soo Cho, and Jong-Shik Shin. https://doi.org/10.1021/acscatal.6b03242
[51] Spectrophotometric Assay for Sensitive Detection of Glycerol Dehydratase Activity Using Aldehyde Dehydrogenase, Journal of Bioscience and Bioengineering
Park, Eul-Soo, Sunghoon Park, and Jong-Shik Shin. https://doi.org/10.1016/j.jbiosc.2016.12.002
[50] A Facile Method to Determine Intrinsic Kinetic Parameters of ω-Transaminase Displaying Substrate Inhibition, Journal of Molecular Catalysis B: Enzymatic
Han, Sang-Woo, and Jong-Shik Shin. https://doi.org/10.1016/j.molcatb.2017.05.001
2015
[49] Preparation of d -Threonine by Biocatalytic Kinetic Resolution, Journal of Molecular Catalysis B: Enzymatic
Han, Sang-Woo, and Jong-Shik Shin. https://doi.org/10.1016/j.molcatb.2015.09.011
[48] Active-Site Engineering of ω-Transaminase for Production of Unnatural Amino Acids Carrying a Side Chain Bulkier than an Ethyl Substituent, Applied and Environmental Microbiology
Han, Sang-Woo, Eul-Soo Park, Joo-Young Dong, and Jong-Shik Shin. https://doi.org/10.1128/aem.01533-15
[47] Biocatalytic Cascade Reactions for Asymmetric Synthesis of Aliphatic Amino Acids in a Biphasic Reaction System, Journal of Molecular Catalysis B: Enzymatic
ark, Eul-Soo, and Jong-Shik Shin. https://doi.org/10.1016/j.molcatb.2015.07.011
[46] Expanding Substrate Specificity of ω-Transaminase by Rational Remodeling of a Large Substrate-Binding Pocket, Advanced Synthesis & Catalysis
Han, Sang-Woo, Eul-Soo Park, Joo-Young Dong, and Jong-Shik Shin. https://doi.org/10.1002/adsc.201500239
[45] Mechanism-Guided Engineering of ω-Transaminase to Accelerate Reductive Amination of Ketones, Advanced Synthesis & Catalysis
Han, Sang-Woo, Eul-Soo Park, Joo-Young Dong, and Jong-Shik Shin. https://doi.org/10.1002/adsc.201500211
2014
[44] Highly Efficient I2-Free Solid-State Dye-Sensitized Solar Cells Fabricated with Polymerized Ionic Liquid and Graft Copolymer-Directed Mesoporous Film, Electrochemistry Communications
Chi, Won Seok, Jong Kwan Koh, Sung Hoon Ahn, Jong-Shik Shin, Hyungju Ahn, Du Yeol Ryu, and Jong Hak Kim. https://doi.org/10.1016/j.elecom.2011.08.005
[43] Metabolically Driven Equilibrium Shift of Asymmetric Amination of Ketones by ω-Transaminase Using Alanine as an Amino Donor, Bioscience, Biotechnology, and Biochemistry
Han, Sang-Woo, and Jong-Shik Shin. https://doi.org/10.1080/09168451.2014.930328
[42] Deracemization of Amino Acids by Coupling Transaminases of Opposite Stereoselectivity, Advanced Synthesis & Catalysis
Park, Eul-Soo, and Jong-Shik Shin. https://doi.org/10.1002/adsc.201400185
[41] Structural Determinants for the Non-Canonical Substrate Specificity of the ω-Transaminase FromParacoccus Denitrificans, Advanced Synthesis & Catalysis
Park, Eul-Soo, Sae-Rom Park, Sang-Woo Han, Joo-Young Dong, and Jong-Shik Shin. https://doi.org/10.1002/adsc.201300786.
[40] Active Site Model of (R)-Selective ω-Transaminase and Its Application to the Production of d-Amino Acids, Applied Microbiology and Biotechnology
Park, Eul-Soo, Joo-Young Dong, and Jong-Shik Shin. https://doi.org/10.1007/s00253-013-4846-5
2013
[39] Biocatalytic Asymmetric Synthesis of Unnatural Amino Acids through the Cascade Transfer of Amino Groups from Primary Amines onto Keto Acids, ChemCatChem
Park, Eul-Soo, Joo-Young Dong, and Jong-Shik Shin. https://doi.org/10.1002/cctc.201300571
[38] ω-Transaminase-Catalyzed Asymmetric Synthesis of Unnatural Amino Acids Using Isopropylamine as an Amino Donor, Organic & Biomolecular Chemistry
Park, Eul-Soo, Joo-Young Dong, and Jong-Shik Shin. https://doi.org/10.1039/c3ob40495a
[37] ω-Transaminase from Ochrobactrum Anthropi Is Devoid of Substrate and Product Inhibitions, Applied and Environmental Microbiology
Park, Eul-Soo, and Jong-Shik Shin. https://doi.org/10.1128/aem.03811-12
[36] One-Pot Production of Enantiopure Alkylamines and Arylalkylamines of Opposite Chirality Catalyzed by ω-Transaminase, ChemCatChem
Park, Eul-Soo, M. Shaheer Malik, Joo-Young Dong, and Jong-Shik Shin. https://doi.org/10.1002/cctc.201300052
2012
[35] Probing Translation Initiation through Ligand Binding to the 5′ MRNA Coding Region, ChemBioChem
Jo, Joon-Jung, Joo-Hee Kim, and Jong-Shik Shin. https://doi.org/10.1002/cbic.201200432.
[34] ω-Transaminase-Catalyzed Kinetic Resolution of Chiral Amines Using L-Threonine as an Amino Acceptor Precursor, Green Chemistry
Malik, M. Shaheer, Eul-Soo Park, and Jong-Shik Shin. https://doi.org/10.1039/c2gc35615e
[33] Facile Fabrication of Vertically Aligned TiO2 Nanorods with High Density and Rutile/Anatase Phases on Transparent Conducting Glasses: High Efficiency Dye-Sensitized Solar Cells, Journal of Materials Chemistry
Park, Jung Tae, Rajkumar Patel, Harim Jeon, Dong Jun Kim, Jong-Shik Shin, and Jong Hak Kim. https://doi.org/10.1039/c2jm13770d
[32] Graft Copolymer Templated Synthesis of Mesoporous MgO/TiO2 Mixed Oxide Nanoparticles and Their CO2 Adsorption Capacities, Colloids and Surfaces A: Physicochemical and Engineering Aspects
Jeon, Harim, Yoon Jae Min, Sung Hoon Ahn, Seok-Min Hong, Jong-Shik Shin, Jong Hak Kim, and Ki Bong Lee. https://doi.org/10.1016/j.colsurfa.2012.08.009
[31] Pretreatment Of Cellulosic Waste Sawdust Into Reducing Sugars Using Mercerization And Etherification, BioResources
Kim, Beomsoo, Ishan Gulati, Jinwon Park, and Jong-Shik Shin. https://doi.org/10.15376/biores.7.4.5152-5166
[30] Features and Technical Applications of ω-Transaminases, Applied Microbiology and Biotechnology
Malik, M. Shaheer, Eul-Soo Park, and Jong-Shik Shin. https://doi.org/10.1007/s00253-012-4103-3
[29] Molecular Determinants for Substrate Selectivity of ω-Transaminases, Applied Microbiology and Biotechnology
Park, Eul-Soo, Minji Kim, and Jong-Shik Shin. https://doi.org/10.1007/s00253-011-3584-9
2011
[28] Fabrication of 3D Interconnected Porous TiO2nanotubes Templated by Poly(Vinyl Chloride-g-4-Vinyl Pyridine) for Dye-Sensitized Solar Cells, Nanotechnology
Koh, Joo Hwan, Jong Kwan Koh, Jin Ah Seo, Jong-Shik Shin, and Jong Hak Kim. https://doi.org/10.1088/0957-4484/22/36/365401
[27] Free Energy Analysis Of ω-Transaminase Reactions To Dissect How The Enzyme Controls The Substrate Selectivity, Enzyme And Microbial Technology
Park, Eul-Soo, and Jong-Shik Shin. doi:10.1016/j.enzmictec.2011.06.019.
2010
[26] One-Pot Conversion of L-Threonine into L-Homoalanine: Biocatalytic Production of an Unnatural Amino Acid from a Natural One, Advanced Synthesis & Catalysis
Park, Eulsoo, Minji Kim, and Jong-Shik Shin. https://doi.org/10.1002/adsc.201000601
[25] Self-Assembled Nucleic Acid Nanoparticles Capable of Controlled Disassembly in Response to a Single Nucleotide Mismatch, Biomacromolecules
Kim, Jandi, Cho-Ah Im, Yongchul Jung, Altaf Qazi, and Jong-Shik Shin. https://doi.org/10.1021/bm100368d.
[24] Probing the Transition State for Nucleic Acid Hybridization Using Φ-Value Analysis, Biochemistry
Kim, Jandi, and Jong-Shik Shin. https://doi.org/10.1021/bi902047x.
2009
[23] Construction of Intragenic Synthetic Riboswitches for Detection of a Small Molecule, Biotechnology Letters
Jo, Joon-Jung, and Jong-Shik Shin. https://doi.org/10.1007/s10529-009-0058-6.
[22] Transaminase-Catalyzed Asymmetric Synthesis of l-2-Aminobutyric Acid from Achiral Reactants, Biotechnology Letters
Shin, Jong-Shik, and Byung-Gee Kim. https://doi.org/10.1007/s10529-009-0057-7.
[21] Single-Fluorophore Monitoring of DNA Hybridization for Investigating the Effect of Secondary Structure on the Nucleation Step, Biochemical and Biophysical Research Communications
Jo, Joon-Jung, Min-Ji Kim, Jung-Tae Son, Jandi Kim, and Jong-Shik Shin. https://doi.org/10.1016/j.bbrc.2009.04.140.
2006
[20] Viscous Drag as the Source of Active Site Perturbation during Protease Translocation: Insights into How Inhibitory Processes Are Controlled by Serpin Metastability, Journal of Molecular Biology
Shin, Jong-Shik, and Myeong-Hee Yu. https://doi.org/10.1016/j.jmb.2006.03.045.
[19] Misfolding-assisted selection of stable protein variants using phage displays, BMB Reports
Shin, Jong-Shik, Seung-Hyun Ryu, Cheol-Ju Lee, and Myeong-Hee Yu. https://doi.org/10.5483/bmbrep.2006.39.1.055.
2004
[18] A synthetic DNA walker for molecular transport, Journal of the American Chemical Society
Shin, Jong-Shik, and Niles A. Pierce. https://doi.org/10.1021/ja047543j.
2003
[17] Rewritable memory by controllable nanopatterning of DNA, Nano Letters
Shin, Jong-Shik, and Niles A. Pierce. https://doi.org/10.1021/nl049658r.
[16] Purification, Characterization, and Molecular Cloning of a Novel Amine:Pyruvate Transaminase from Vibrio Fluvialis JS17, Applied Microbiology and Biotechnology
Shin, J.-S., H. Yun, J.-W. Jang, I. Park, and B.-G. Kim. https://doi.org/10.1007/s00253-003-1250-6.
[15] Substrate inhibition mode of ω-transaminase from Vibrio fluvialis JS17 is dependent on the chirality of substrate, Biotechnology and Bioengineering
Shin, Jong-Shik, and Byung-Gee Kim. https://doi.org/10.1002/bit.10165.
2002
[14] Exploring the active site of amine:pyruvate aminotransferase based on substrate structure-reactivity relationship: How the enzyme controls substrate specificity and stereoselectivity, The Journal of Organic Chemistry
Shin, Jong-Shik, and Byung-Gee Kim. https://doi.org/10.1021/jo016115i.
[13] Kinetic dissection of a1-antitrypsin inhibition mechanism, Journal Of Biological Chemistry
Shin, Jong-Shik, and Myeong-Hee Yu. doi:10.1074/jbc.m111168200.
[12] Revisiting the effect of water content on enzymatic peptide synthesis in non-aqueous medium, Biotechnology Letters
Shin, Jong-Shik, and Byung-Gee Kim.doi:10.1023/a:1020952109068.
2001
[11] Kinetic resolution of chiral amines with ω-transaminase using enzyme membrane reactor, Biotechnology And Bioengineering
Shin, Jong-Shik, Byung-Gee Kim, Andreas Liese, and Christian Wandrey. doi:10.1002/bit.1050.
[10] Comparison of the ω-transaminases from different microorganisms and application to production of chiral amines, Bioscience, Biotechnology, And Biochemistry
Shin, Jong-Shik, and Byung-Gee KIM. doi:10.1271/bbb.65.1782.
[9] Kinetic resolution of chiral amines using packed-bed reactor, Enzyme And Microbial Technology
Shin, Jong-Shik, Byung-Gee Kim, and Dong-Hoon Shin. doi:10.1016/s0141-0229(01)00382-9.
2000
[8] Improving lipase enantioselectivity in organic solvents by forming substrate salts with chiral agents, Biotechnology and Bioengineering
Shin, Jong-Shik, Susana Luque, and Alexander M. Klibanov. https://doi.org/10.1002/1097-0290(20000905)69:5<577::aid-bit12>3.0.co;2-y.
[7] Protease-catalyzed tripeptide (RGD) synthesis, Enzyme and Microbial Technology
So, Jin-Eon, Jong-Shik Shin, and Byung-Gee Kim. https://doi.org/10.1016/s0141-0229(99)00132-5.
1999
[6] Asymmetric synthesis of chiral amines with ω-transaminase, Biotechnology and Bioengineering
Shin, Jong-Shik, and Byung-Gee Kim. https://doi.org/10.1002/(sici)1097-0290(19991020)65:2<206::aid-bit11>3.0.co;2-9.
[5] Modeling of the kinetic resolution of α-methylbenzylamine with ω-transaminase in a two-liquid-phase system, Enzyme and Microbial Technology
Shin, Jong-Shik, and Byung-Gee Kim. https://doi.org/10.1016/s0141-0229(99)00067-8.
1998
[4] Kinetic modeling of ω-transamination for enzymatic kinetic resolution of α-methylbenzylamine, Biotechnology and Bioengineering
Shin, Jong-Shik, and Byung-Gee Kim. https://doi.org/10.1002/(sici)1097-0290(19981205)60:5<534::aid-bit3>3.0.co;2-l.
1997
[3] Kinetic resolution of α-methylbenzylamine with ω-transaminase screened from soil microorganisms: application of a biphasic system to overcome product inhibition, Biotechnology and Bioengineering
Shin, Jong-Shik, and Byung-Gee Kim. https://doi.org/10.1002/(sici)1097-0290(19970720)55:2<348::aid-bit12>3.0.co;2-d.
1996
[2] Spectrophotometric assay using streptavidin-alkaline phosphatase conjugate for studies on the proteolysis of polymer bead-bound peptides, Analytical Biochemistry
Shin, J.s., B.g. Kim, D.h. Kim, and Y.s. Lee. https://doi.org/10.1006/abio.1996.0124.
[1] Optical resolution of racemic 1-phenylethylamine catalyzed by aminotransferase and dehydrogenase, Annals of the New York Academy of Sciences
Shin, Jong-Shik, and Byung-Gee Kim. https://doi.org/10.1111/j.1749-6632.1996.tb33280.x.