Literature DB >> 18258209

Heme-iron oxygenases: powerful industrial biocatalysts?

Mattijs K Julsing1, Sjef Cornelissen, Bruno Bühler, Andreas Schmid.   

Abstract

Are cytochrome P450 enzymes powerful industrial biocatalysts? Next to market demands, well-defined enzyme functionalities and process parameters allow generalizations on the basis of process windows. These can provide useful guidelines for the design of improved biocatalysts. Oxygenase-catalyzed reactions are of special interest for selective C-H bond oxidation. The versatile class of cytochrome P450 mono-oxygenases attracts particular attention, and impressive advances have been achieved with respect to mechanistic insight, enzyme activity, stability, and specificity. Recent major achievements include significant increases in productivities, yields, and rates of catalytic turnover as well as modification of substrate specificity and efficient multistep reactions in whole-cell biocatalysts. For some biocatalysts, these parameters are already of an industrially useful magnitude.

Mesh:

Substances:

Year:  2008        PMID: 18258209     DOI: 10.1016/j.cbpa.2008.01.029

Source DB:  PubMed          Journal:  Curr Opin Chem Biol        ISSN: 1367-5931            Impact factor:   8.822


  29 in total

Review 1.  Enzymatic functionalization of carbon-hydrogen bonds.

Authors:  Jared C Lewis; Pedro S Coelho; Frances H Arnold
Journal:  Chem Soc Rev       Date:  2010-11-15       Impact factor: 54.564

2.  Regioselective aromatic hydroxylation of quinaldine by water using quinaldine 4-oxidase in recombinant Pseudomonas putida.

Authors:  F Ozde Utkür; Sushil Gaykawad; Bruno Bühler; Andreas Schmid
Journal:  J Ind Microbiol Biotechnol       Date:  2010-10-02       Impact factor: 3.346

3.  Production of drug metabolites by immobilised Cunninghamella elegans: from screening to scale up.

Authors:  Laura Quinn; Rita Dempsey; Eoin Casey; Ayla Kane; Cormac D Murphy
Journal:  J Ind Microbiol Biotechnol       Date:  2015-02-10       Impact factor: 3.346

Review 4.  Biological roles of cytochrome P450 1A1, 1A2, and 1B1 enzymes.

Authors:  Yeo-Jung Kwon; Sangyun Shin; Young-Jin Chun
Journal:  Arch Pharm Res       Date:  2021-01-23       Impact factor: 4.946

Review 5.  Use of chemical auxiliaries to control p450 enzymes for predictable oxidations at unactivated C-h bonds of substrates.

Authors:  Karine Auclair; Vanja Polic
Journal:  Adv Exp Med Biol       Date:  2015       Impact factor: 2.622

Review 6.  Controlling substrate specificity and product regio- and stereo-selectivities of P450 enzymes without mutagenesis.

Authors:  Vanja Polic; Karine Auclair
Journal:  Bioorg Med Chem       Date:  2014-06-25       Impact factor: 3.641

7.  Comparison of microbial hosts and expression systems for mammalian CYP1A1 catalysis.

Authors:  Sjef Cornelissen; Mattijs K Julsing; Andreas Schmid; Bruno Bühler
Journal:  J Ind Microbiol Biotechnol       Date:  2011-08-24       Impact factor: 3.346

8.  Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins.

Authors:  Fangfang Zhong; George P Lisi; Daniel P Collins; John H Dawson; Ekaterina V Pletneva
Journal:  Proc Natl Acad Sci U S A       Date:  2014-01-07       Impact factor: 11.205

9.  Biosynthetic pathway for the cyanide-free production of phenylacetonitrile in Escherichia coli by utilizing plant cytochrome P450 79A2 and bacterial aldoxime dehydratase.

Authors:  Yuta Miki; Yasuhisa Asano
Journal:  Appl Environ Microbiol       Date:  2014-08-29       Impact factor: 4.792

10.  Cytochrome P450 125 (CYP125) catalyses C26-hydroxylation to initiate sterol side-chain degradation in Rhodococcus jostii RHA1.

Authors:  Kamila Z Rosłoniec; Maarten H Wilbrink; Jenna K Capyk; William W Mohn; Martin Ostendorf; Robert van der Geize; Lubbert Dijkhuizen; Lindsay D Eltis
Journal:  Mol Microbiol       Date:  2009-10-15       Impact factor: 3.501

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.