Journal article icon

Journal article

Substrate analogues and inhibition of ACC oxidase: Conversion of D-valine to iso-butanal

Abstract:
Amino acids and their hydroxamates were studied as inhibitors of purified recombinant 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase (tomato). Neither L-valine, L-alanine, L- nor D-isoleucine displayed inhibition, but D-valine and D- alanine were weak inhibitors of ACC oxidase catalysed conversion of ACC to ethylene. GC-MS analysis showed that D-valine was converted to iso-butanal. In contrast to studies using native ACC oxidase (apple), inhibition of recombinant ACC oxidase (tomato) by amino acid hydroxamates appears to result (at least predominantly) from chelation of free iron in solution.
Publication status:
Published

Actions

Access Document

Publisher copy:
10.1016/S0031-9422(97)00965-5

Authors

More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author


Journal:
PHYTOCHEMISTRY More from this journal
Volume:
48
Issue:
4
Pages:
619-624
Publication date:
1998-06-01
DOI:
ISSN:
0031-9422


Language:
English
Keywords:
Pubs id:
pubs:36562
UUID:
uuid:14914efc-bd75-4689-abdc-275e8a3df875
Local pid:
pubs:36562
Source identifiers:
36562
Deposit date:
2012-12-19
ARK identifier:

Terms of use


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP