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Mapping the hydrophobic substrate binding site of phenylalanine ammonia lyase from Petroselinum crispum

Abstract:

Modification of the hydrophobic binding pocket of phenylalanine ammonia-lyase from Petroselinum crispum (PcPAL) enables increased activity and selectivity towards phenylalanines and cinnamic acids mono-substituted with both electron donating (-CH3, -OCH3) and electron withdrawing (-CF3, -Br) groups at all positions (o-, m-, p-) of their aromatic ring. The results reveal specific residues involved in accommodating substituents at o-, m-, p-positions of the substrate’s phenyl ring. The predicte...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1021/acscatal.9b02108

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Oxford college:
Pembroke College
Role:
Author
More from this funder
Name:
Swiss National Science Foundation
Grant:
IZ11Z0_166543
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Name:
National Authority for Scientific Research and Innovation (ANCSI) and European Regional Development Fund
Grant:
ID P37_273, Cod MySMIS 103413
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Name:
Wellcome Trust
Grant:
106244/Z/14/Z
More from this funder
Name:
Medical Research Council
Grant:
MR/P007503/1
More from this funder
Name:
Medical Research Foundation
Grant:
MRF-145-0004-TPG-AVISO
Publisher:
American Chemical Society
Journal:
ACS Catalysis More from this journal
Volume:
9
Issue:
9
Pages:
8825-8834
Publication date:
2019-08-13
Acceptance date:
2019-08-13
DOI:
EISSN:
2155-5435
Language:
English
Keywords:
Pubs id:
pubs:1046712
UUID:
uuid:feadd683-cd09-442c-8b42-7dca03886080
Local pid:
pubs:1046712
Source identifiers:
1046712
Deposit date:
2019-08-21

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