scholarly journals A Cerulenin Insensitive Short Chain 3-Ketoacyl-Acyl Carrier Protein Synthase in Spinacia oleracea Leaves

1989 ◽  
Vol 90 (1) ◽  
pp. 41-44 ◽  
Author(s):  
Jan G. Jaworski ◽  
Richard C. Clough ◽  
Susan R. Barnum
Keyword(s):  
Spinacia Oleracea ◽  
Acyl Carrier Protein ◽  
Short Chain ◽  
Carrier Protein

scholarly journals Plant holo-(acyl carrier protein) synthase

1988 ◽  
Vol 252 (1) ◽  
pp. 39-45 ◽  
Author(s):  
S A Elhussein ◽  
J A Miernyk ◽  
J B Ohlrogge
Keyword(s):  
Spinacia Oleracea ◽  
Acyl Carrier Protein ◽  
Ricinus Communis ◽  
Plant Cells ◽  
Gel Permeation Chromatography ◽  
Carrier Protein ◽  
Improved Method ◽  
Ph Optimum ◽  
Spinach Leaf

1. An improved method was developed for the assay of plant holo-(acyl carrier protein) synthase activity, using Escherichia coli acyl-(acyl carrier protein) synthetase as a coupling enzyme. 2. Holo-(acyl carrier protein) synthase was partially purified from spinach (Spinacia oleracea) leaves by a combination of (NH4)2SO4 fractionation and anion-exchange and gel-permeation chromatography. 3. The partially purified enzyme had a pH optimum of 8.2 and Km values of 2 microM, 72 microM and 3 mM for apo-(acyl carrier protein), CoA and Mg2+ respectively. Synthase activity was inhibited in vitro by the reaction product 3′,5′-ADP. 4. Results from the fractionation of spinach leaf and developing castor-oil-seed (Ricinus communis) endosperm cells were consistent with a cytosolic localization of holo-(acyl carrier protein) synthase activity in plant cells.

scholarly journals The fabJ-encoded beta-ketoacyl-[acyl carrier protein] synthase IV from Escherichia coli is sensitive to cerulenin and specific for short-chain substrates.

1994 ◽  
Vol 91 (23) ◽  
pp. 11027-11031 ◽  
Author(s):  
M. Siggaard-Andersen ◽  
M. Wissenbach ◽  
J. A. Chuck ◽  
I. Svendsen ◽  
J. G. Olsen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Acyl Carrier Protein ◽  
Short Chain ◽  
Carrier Protein
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