Martin Schürmann

ORCID: 0000-0003-3286-122X
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About
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Research Areas
  • Enzyme Catalysis and Immobilization
  • Microbial Metabolic Engineering and Bioproduction
  • Carbohydrate Chemistry and Synthesis
  • Amino Acid Enzymes and Metabolism
  • Enzyme Structure and Function
  • Chemical Synthesis and Analysis
  • Biochemical and biochemical processes
  • Microbial Metabolism and Applications
  • Pharmacogenetics and Drug Metabolism
  • Biochemical and Molecular Research
  • Steroid Chemistry and Biochemistry
  • Plant biochemistry and biosynthesis
  • biodegradable polymer synthesis and properties
  • Viral Infectious Diseases and Gene Expression in Insects
  • Oxidative Organic Chemistry Reactions
  • Enzyme Production and Characterization
  • Cancer Research and Treatments
  • Chemistry and Chemical Engineering
  • Chemical Reactions and Isotopes
  • Phagocytosis and Immune Regulation
  • Biofuel production and bioconversion
  • Enhanced Oil Recovery Techniques
  • Metal-Catalyzed Oxygenation Mechanisms
  • Pancreatitis Pathology and Treatment
  • Glycosylation and Glycoproteins Research

Society for Chemical Engineering and Biotechnology
2024

Institute of Organic Synthesis
2019

DSM (Netherlands)
2007-2018

Dynamic Structures and Materials (United States)
2013-2017

Innosys (United States)
2017

Netherlands Leprosy Relief
2015

University of Stuttgart
2007

Forschungszentrum Jülich
2002

Abstract Aldolases are emerging as powerful and cost efficient tools for the industrial synthesis of chiral molecules. They catalyze enantioselective carbon‐carbon bond formations, generating up to two centers under mild reaction conditions. Despite their versatility, narrow substrate ranges enzyme inactivation conditions represented major obstacles large‐scale applications aldolases. In this study we applied directed evolution optimize Escherichia coli 2‐deoxy‐ D ‐ribose 5‐phosphate...

10.1002/biot.200600020 article EN Biotechnology Journal 2006-05-01

The potential of biotechnology by means biocatalysis or biosynthesis in organic synthesis is far from being fully exploited. For this reason a group life science companies active pharmaceuticals, flavour and fragrance, vitamin fine chemicals businesses describe some examples the use enzymes industrial discuss why are still exception rather than rule synthesis.

10.1039/c2cy20350b article EN Catalysis Science & Technology 2012-08-10

Nylon-6 is a bulk polymer used for many applications. It consists of the non-natural building block 6-aminocaproic acid, linear form caprolactam. Via retro-synthetic approach, two synthetic pathways were identified fermentative production acid. Both require yet unreported novel biocatalytic steps. We demonstrated proof these bioconversions by in vitro enzyme assays with set selected candidate proteins expressed Escherichia coli. One biosynthetic starts 2-oxoglutarate and contains ketoacid...

10.1021/acssynbio.5b00129 article EN ACS Synthetic Biology 2015-10-29

We created a novel chimeric amine dehydrogenase (AmDH) via domain shuffling of two parent AmDHs ('L- and F-AmDH'), which in turn had been generated from leucine phenylalanine DH, respectively. Unlike the proteins, AmDH ('cFL-AmDH') catalyzes amination acetophenone to (R)-methylbenzylamine adamantylmethylketone adamantylethylamine.

10.1039/c4cc06527a article EN Chemical Communications 2014-10-10

Chiral amines are important building blocks for the synthesis of pharmaceutical products, fine chemicals, and agrochemicals. ω-Transaminases able to directly synthesize enantiopure chiral by catalysing transfer an amino group from a primary donor carbonyl acceptor with pyridoxal 5'-phosphate (PLP) as cofactor. In nature, (S)-selective amine transaminases more abundant than (R)-selective enzymes, therefore information concerning their structures is available. Here, we present crystal...

10.1371/journal.pone.0087350 article EN cc-by PLoS ONE 2014-01-30

Hydratases provide access to secondary and tertiary alcohols by regio- and/or stereospecifically adding water carbon-carbon double bonds. Thereby, hydroxy groups are introduced without the need for costly cofactor recycling, that makes this approach highly interesting on an industrial scale. Here we present first crystal structure of a recombinant oleate hydratase originating from Elizabethkingia meningoseptica in presence flavin adenine dinucleotide (FAD). A structure-based mutagenesis...

10.1002/cbic.201500269 article EN other-oa ChemBioChem 2015-06-15

The development of P450 platform technology has enabled the sustainable production an oxygenated intermediate, 4-hydroxy-α-isophorone, on kilogram scale. Application a cytochrome enzyme resulted in unprecedented product concentration 10 g/L and space–time yield 1.5 g/L/h. These findings are highly relevant for economical evaluation and, additionally, provide access to alternative cost-effective route toward 4-hydroxy-α-isophorone.

10.1021/acs.oprd.5b00282 article EN Organic Process Research & Development 2016-03-14

Invited for this month's cover is the Working Group Sustainable Chemistry of European Society Applied Biocatalysis (ESAB). The image shows significant contributions to science, industry, society, and environment as a technology first choice in 21st century. Perspective itself available at 10.1002/cssc.202102709.

10.1002/cssc.202200709 article EN ChemSusChem 2022-04-21

Recent advances in bioeconomy allow a holistic view of existing and new process chains enable novel production routines continuously advanced by academia industry. All this progress benefits from growing number prediction tools that have found their way into the field. For example, automated genome annotations, for building model structures proteins, structural protein methods such as AlphaFold2

10.1002/cbic.202300863 article EN cc-by ChemBioChem 2024-05-07

Dynamic and successful: The asymmetric synthesis of 2-amino-1-phenylethanol was achieved by aminomethylation benzaldehyde in the presence two enzymes L-threonine aldolase L-tyrosine decarboxylase a novel one-pot, two-enzyme process (see scheme). A modified method with three led to enantioenriched amino alcohol very high yield. Supporting information for this article is available on WWW under http://www.wiley-vch.de/contents/jc_2002/2007/z604142_s.pdf or from author. Please note: publisher...

10.1002/anie.200604142 article EN Angewandte Chemie International Edition 2007-01-24

Soluble water-forming NAD(P)H oxidases constitute a promising NAD(P)(+) regeneration method as they only need oxygen cosubstrate and produce water sole byproduct. Moreover, the thermodynamic equilibrium of O2 reduction is valuable driving force for mostly energetically unfavorable biocatalytic oxidations. Here, we present generation an oxidase with high activity both cofactors, NADH NADPH. Starting from strictly specific Streptococcus mutans 2 several rationally designed cofactor binding...

10.5936/csbj.201402005 article EN cc-by Computational and Structural Biotechnology Journal 2014-02-01

Abstract Transaminases are useful biocatalysts for the production of amino acids and chiral amines as intermediates a broad range drugs fine chemicals. Here, we describe discovery characterisation new transaminases from microorganisms which were enriched in selective media containing ( R )-amines sole nitrogen source. While most candidate proteins clearly assigned to known subgroups fold IV family PLP-dependent enzymes by sequence analysis their substrate specificity, some them did not fit...

10.1038/srep38183 article EN cc-by Scientific Reports 2016-12-01

Membrane-anchored cytochrome P450 enzymes (CYPs) are a versatile and interesting class of for industrial applications, as they capable regio- stereoselectively hydroxylating hydrophobic molecules. However, CYP activity requires sufficient levels suitable reductases (CPRs) regeneration catalytic capacity, which is bottleneck in many applications. Searching positive effectors membrane-anchored CYP/CPR function, we transformed screened selected strains from Saccharomyces cerevisiae knockout...

10.1002/biot.201400780 article EN Biotechnology Journal 2015-01-12

Screening of 60 transaminases using three different amine donors found that the ω-transaminase from Vibrio fluvialis together with (S)-α-methylbenzylamine to be most promising combination deliver desired (S)-1-(5-fluoropyrimidin-2-yl)-ethylamine (2) in almost quantitative conversion. The process was further improved by addition immiscible organic solvents toluene identified as suitable concerning distribution reactants without negatively impacting performance biocatalyst. Further...

10.1021/op400131h article EN Organic Process Research & Development 2013-08-21

Amine transaminases are frequently used for the production of chiral amines starting from prochiral ketones. These can be applied as active pharmaceutical ingredients or drug precursors. However, there still limitations to use amine when it comes bulky ketone substrates, such biaryl Using data mining, an (R)-selective transaminase Exophiala xenobiotica was identified which naturally converts substrates corresponding with up 85% conversion and excellent enantioselectivity (>99% ee). Its...

10.1021/acscatal.8b04524 article EN ACS Catalysis 2018-12-20
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