Cover Picture: Phenylalanine Ammonia‐Lyase‐Catalyzed Deamination of an Acyclic Amino Acid: Enzyme Mechanistic Studies Aided by a Novel Microreactor Filled with Magnetic Nanoparticles (ChemBioChem 16/2015). Issue 16 (21st October 2015)
- Record Type:
- Journal Article
- Title:
- Cover Picture: Phenylalanine Ammonia‐Lyase‐Catalyzed Deamination of an Acyclic Amino Acid: Enzyme Mechanistic Studies Aided by a Novel Microreactor Filled with Magnetic Nanoparticles (ChemBioChem 16/2015). Issue 16 (21st October 2015)
- Main Title:
- Cover Picture: Phenylalanine Ammonia‐Lyase‐Catalyzed Deamination of an Acyclic Amino Acid: Enzyme Mechanistic Studies Aided by a Novel Microreactor Filled with Magnetic Nanoparticles (ChemBioChem 16/2015)
- Authors:
- Weiser, Diána
Bencze, László Csaba
Bánóczi, Gergely
Ender, Ferenc
Kiss, Róbert
Kókai, Eszter
Szilágyi, András
Vértessy, Beáta G.
Farkas, Ödön
Paizs, Csaba
Poppe, László - Abstract:
- <abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The cover picture shows</bold> phenylalanine ammonia‐lyase (PAL) immobilized on magnetic nanoparticles (MNPs) and its use in a magnetic microfluidic reactor with in‐line UV detection to confirm for the first time that propargylglycine could be reversibly and stereospecifically transformed by PAL. The authors describe how a non‐aromatic, acyclic amino acid was transformed to (<italic>E</italic>)‐pent‐2‐ene‐4‐ynoate. Experiments and QM/MM calculations showed that this was only possible through a covalent intermediate with a bond between the amino group of the substrate and the MIO prosthetic group. Their findings open up new opportunities for the application of the MIO enzyme toolbox towards non‐aromatic acyclic substrates. More details can be found in the Communication by C. Paizs, L. Poppe et al. on <bold>page 2283 in Issue 16, 2015</bold> (DOI: <ext-link ext-link-type="uri" xlink:href="http://dx.doi.org/10.1002/cbic.201500444" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">10.1002/cbic.201500444</ext-link>).<graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgkv84q9xz" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></p> </abstract>
- Is Part Of:
- Chembiochem. Volume 16:Issue 16(2015)
- Journal:
- Chembiochem
- Issue:
- Volume 16:Issue 16(2015)
- Issue Display:
- Volume 16, Issue 16 (2015)
- Year:
- 2015
- Volume:
- 16
- Issue:
- 16
- Issue Sort Value:
- 2015-0016-0016-0000
- Page Start:
- 2257
- Page End:
- 2257
- Publication Date:
- 2015-10-21
- Subjects:
- Biochemistry -- Periodicals
Molecular biology -- Periodicals
Pharmaceutical chemistry -- Periodicals
572 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1439-7633 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/cbic.201500520 ↗
- Languages:
- English
- ISSNs:
- 1439-4227
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3133.490980
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 4328.xml