Karl Gruber

Research interests

Publications

• Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2

  Scientific Reports · 2021 · 10.1038/s41598-021-83761-5

• Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2

  Scientific Reports · 2021 · 10.1038/s41598-021-83761-5

• PpEst is a novel PBAT degrading polyesterase identified by proteomic screening of Pseudomonas pseudoalcaligenes

  Applied Microbiology and Biotechnology · 2016 · 10.1007/s00253-016-7992-8

• Improving enzymatic polyurethane hydrolysis by tuning enzyme sorption

  Polymer Degradation and Stability · 2016 · 10.1016/j.polymdegradstab.2016.02.025

• Hydrolysis of synthetic polyesters by Clostridium botulinum esterases

  Biotechnology and Bioengineering · 2015 · 10.1002/bit.25874

• Oxidation of Monolignols by Members of the Berberine Bridge Enzyme Family Suggests a Role in Plant Cell Wall Metabolism

  Journal of Biological Chemistry · 2015 · https://doi.org/10.1074/jbc.m115.659631

• Characterization of a poly(butylene adipate-co-terephthalate)-hydrolyzing lipase from Pelosinus fermentans

  Applied Microbiology and Biotechnology · 2015 · 10.1007/s00253-015-7031-1

• Hydrolysis of synthetic polyesters by Clostridium botulinum esterases

  Biotechnology and Bioengineering · 2015 · 10.1002/bit.25874

• Characterization of a poly(butylene adipate-co-terephthalate)-hydrolyzing lipase from Pelosinus fermentans

  Applied Microbiology and Biotechnology · 2015 · 10.1007/s00253-015-7031-1

• Surface engineering of a cutinase from Thermobifida cellulosilytica for improved polyester hydrolysis

  Biotechnology and Bioengineering · 2013 · 10.1002/bit.24930

• Fusion of Binding Domains to Thermobifida cellulosilytica Cutinase to Tune Sorption Characteristics and Enhancing PET Hydrolysis

  Biomacromolecules · 2013 · 10.1021/bm400140u

• A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA)

  Polymers · 2012 · 10.3390/polym4010617

• Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from Thermobifida

  Macromolecules · 2011 · https://doi.org/10.1021/ma200949p

• Vitamin B12-derivatives—enzyme cofactors and ligands of proteins and nucleic acids

  Chemical Society Reviews · 2011 · https://doi.org/10.1039/c1cs15118e

• A concerted mechanism for berberine bridge enzyme

  Nature Chemical Biology · 2008 · 10.1038/nchembio.123

• Asymmetric Bioreduction of CC Bonds using Enoate Reductases OPR1, OPR3 and YqjM: Enzyme‐Based Stereocontrol

  Advanced Synthesis & Catalysis · 2008 · 10.1002/adsc.200700458

• A Biocatalytic Henry Reaction—The Hydroxynitrile Lyase from Hevea brasiliensis Also Catalyzes Nitroaldol Reactions

  Angewandte Chemie International Edition · 2006 · 10.1002/anie.200504230

• Long‐distance gene flow and cross‐Andean dispersal of lowland rainforest bees (Apidae: Euglossini) revealed by comparative mitochondrial DNA phylogeography

  Molecular Ecology · 2004 · 10.1111/j.1365-294x.2004.02374.x

• Long‐distance gene flow and cross‐Andean dispersal of lowland rainforest bees (Apidae: Euglossini) revealed by comparative mitochondrial DNA phylogeography

  Molecular Ecology · 2004 · 10.1111/j.1365-294x.2004.02374.x

• The Cofactor of Tetrachloroethene Reductive Dehalogenase of Dehalospirillum multivorans Is Norpseudo‐B12, a New Type of a Natural Corrinoid

  Helvetica Chimica Acta · 2003 · 10.1002/hlca.200390313

• Comprehensive Step‐by‐Step Engineering of an (R)‐Hydroxynitrile Lyase for Large‐Scale Asymmetric Synthesis

  Angewandte Chemie International Edition · 2003 · 10.1002/anie.200352141

• Comprehensive Step‐by‐Step Engineering of an (R)‐Hydroxynitrile Lyase for Large‐Scale Asymmetric Synthesis

  Angewandte Chemie International Edition · 2003 · 10.1002/anie.200352141

• Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B12 Dependent Enzyme Glutamate Mutase

  Angewandte Chemie International Edition · 2001 · 10.1002/1521-3773(20010917)40:18<3377::aid-anie3377>3.0.co;2-8

• Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights

  Structure · 1999 · 10.1016/s0969-2126(99)80116-6

• Thermophilic Xylanase from Thermomyces lanuginosus : High-Resolution X-ray Structure and Modeling Studies ,

  Biochemistry · 1998 · 10.1021/bi980864l

• Accurate Structural Data Demystify B12: High-Resolution Solid-State Structure of Aquocobalamin Perchlorate and Structure Analysis of the Aquocobalamin Ion in Solution

  Journal of the American Chemical Society · 1995 · 10.1021/ja00121a022

• Accurate Structural Data Demystify B12: High-Resolution Solid-State Structure of Aquocobalamin Perchlorate and Structure Analysis of the Aquocobalamin Ion in Solution

  Journal of the American Chemical Society · 1995 · 10.1021/ja00121a022

• Direct Evidence for the Conformational Deformation of the Corrin Ring by the Nucleotide Base in Vitamin B12: Synthesis and Solution Spectroscopic and Crystal Structure Analysis of Co.beta.-Cyanoimidazolylcobamide

  Inorganic Chemistry · 1994 · 10.1021/ic00096a043

• S-layer of Lactobacillus helveticus ATCC 12046: isolation, chemical characterization and re-formation after extraction with lithium chloride

  Journal of General Microbiology · 1992 · 10.1099/00221287-138-3-611

Current projects

No projects listed.