Download MendeleyThe X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.
Fisher, M., Kroon, J.T., Martindale, W., Stuitje, A.R., Slabas, A.R., Rafferty, J.B.(2000) Structure 8: 339-347
- PubMed: 10801480
- DOI: https://doi.org/10.1016/s0969-2126(00)00115-5
- Primary Citation of Related Structures:
1EDO - PubMed Abstract:
beta-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.
Organizational Affiliation:
Department of Molecular Biology and Biotechnology, Krebs Institute for Biomolecular Research, The University of Sheffield, Sheffield, S10 2TN, UK.
