Literature DB >> 17607575

Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry.

Thomas Purkarthofer1, Wolfgang Skranc, Christian Schuster, Herfried Griengl.   

Abstract

The application of hydroxynitrile lyases (HNLs) as catalysts for the stereoselective condensation of HCN with carbonyl compounds has been reported as early as 1908. This enzymatic C-C bond coupling reaction furnishes enantiopure cyanohydrins which serve as versatile bifunctional building blocks for chemical synthesis. Screening of natural sources led to the discovery of both (R)- and (S)-selective HNLs, and several distinctly different classes of these enzymes with substantial differences concerning sequence, structure, and mechanism have been found. Especially during the last two centuries, HNLs have been developed into valuable biocatalysts, which can be produced in recombinant form by overexpression in microbial hosts, resulting in the implementation of industrial processes utilizing these enzymes. Recently, protein engineering in combination with in silico methods gave rise to the development of a tailor-made HNL for large-scale manufacturing of a specific target cyanohydrin.

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Year:  2007        PMID: 17607575     DOI: 10.1007/s00253-007-1025-6

Source DB:  PubMed          Journal:  Appl Microbiol Biotechnol        ISSN: 0175-7598            Impact factor:   4.813


  14 in total

1.  Characterization of two bacterial hydroxynitrile lyases with high similarity to cupin superfamily proteins.

Authors:  Zahid Hussain; Romana Wiedner; Kerstin Steiner; Tanja Hajek; Manuela Avi; Bianca Hecher; Angela Sessitsch; Helmut Schwab
Journal:  Appl Environ Microbiol       Date:  2012-01-06       Impact factor: 4.792

2.  Increasing the reaction rate of hydroxynitrile lyase from Hevea brasiliensis toward mandelonitrile by copying active site residues from an esterase that accepts aromatic esters.

Authors:  Jan von Langermann; David M Nedrud; Romas J Kazlauskas
Journal:  Chembiochem       Date:  2014-07-18       Impact factor: 3.164

Review 3.  Biosynthesis of 2-hydroxyisobutyric acid (2-HIBA) from renewable carbon.

Authors:  Thore Rohwerder; Roland H Müller
Journal:  Microb Cell Fact       Date:  2010-02-25       Impact factor: 5.328

4.  Kinetics and mechanism of vanadium catalysed asymmetric cyanohydrin synthesis in propylene carbonate.

Authors:  Michael North; Marta Omedes-Pujol
Journal:  Beilstein J Org Chem       Date:  2010-11-03       Impact factor: 2.883

5.  Discovery and molecular and biocatalytic properties of hydroxynitrile lyase from an invasive millipede, Chamberlinius hualienensis.

Authors:  Mohammad Dadashipour; Yuko Ishida; Kazunori Yamamoto; Yasuhisa Asano
Journal:  Proc Natl Acad Sci U S A       Date:  2015-08-10       Impact factor: 11.205

6.  Activity and enantioselectivity of the hydroxynitrile lyase MeHNL in dry organic solvents.

Authors:  Monica Paravidino; Menno J Sorgedrager; Romano V A Orru; Ulf Hanefeld
Journal:  Chemistry       Date:  2010-07-05       Impact factor: 5.236

7.  Protein evolution analysis of S-hydroxynitrile lyase by complete sequence design utilizing the INTMSAlign software.

Authors:  Shogo Nakano; Yasuhisa Asano
Journal:  Sci Rep       Date:  2015-02-03       Impact factor: 4.379

8.  Hydroxynitrile lyases with α/β-hydrolase fold: two enzymes with almost identical 3D structures but opposite enantioselectivities and different reaction mechanisms.

Authors:  Jennifer N Andexer; Nicole Staunig; Thorsten Eggert; Christoph Kratky; Martina Pohl; Karl Gruber
Journal:  Chembiochem       Date:  2012-07-31       Impact factor: 3.164

9.  Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity.

Authors:  Ingrid Dreveny; Aleksandra S Andryushkova; Anton Glieder; Karl Gruber; Christoph Kratky
Journal:  Biochemistry       Date:  2009-04-21       Impact factor: 3.162

10.  Discovery of a novel (R)-selective bacterial hydroxynitrile lyase from Acidobacterium capsulatum.

Authors:  Romana Wiedner; Mandana Gruber-Khadjawi; Helmut Schwab; Kerstin Steiner
Journal:  Comput Struct Biotechnol J       Date:  2014-07-08       Impact factor: 7.271

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