TY - JOUR
T1 - The X-ray structure of Brassica napus ß-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.
AU - Fisher, M.
AU - Kroon, J.T.M.
AU - Martindale, W.
AU - Stuitje, A.R.
AU - Slabas, A.R.
AU - Rafferty, J.B.
PY - 2000
Y1 - 2000
N2 - Background: β-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. Results: The first crystal structure of BKR has been determined at 2.3 Å resolution in a binary complex with an NADP
AB - Background: β-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. Results: The first crystal structure of BKR has been determined at 2.3 Å resolution in a binary complex with an NADP
UR - https://www.scopus.com/pages/publications/0034656330
UR - https://www.scopus.com/inward/citedby.url?scp=0034656330&partnerID=8YFLogxK
U2 - 10.1016/S0969-2126(00)00115-5
DO - 10.1016/S0969-2126(00)00115-5
M3 - Article
SN - 0969-2126
VL - 8
SP - 339
EP - 347
JO - Structure
JF - Structure
ER -
