The X-ray structure of Brassica napus ß-keto acyl carrier protein reductase and its implications for substrate binding and catalysis.

M. Fisher, J.T.M. Kroon, W. Martindale, A.R. Stuitje, A.R. Slabas, J.B. Rafferty

    Research output: Contribution to JournalArticleAcademicpeer-review

    Abstract

    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
    Original languageEnglish
    Pages (from-to)339-347
    Number of pages9
    JournalStructure
    Volume8
    DOIs
    Publication statusPublished - 2000

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    Acyl Carrier Protein
    Brassica napus
    Catalysis
    Fatty Acid Synthases
    Oxidoreductases
    X-Rays
    NADP
    Polyketides
    Alcohol Dehydrogenase
    Fatty Acids
    Nucleotides
    Enzymes

    Cite this

    Fisher, M. ; Kroon, J.T.M. ; Martindale, W. ; Stuitje, A.R. ; Slabas, A.R. ; Rafferty, J.B. / The X-ray structure of Brassica napus ß-keto acyl carrier protein reductase and its implications for substrate binding and catalysis. In: Structure. 2000 ; Vol. 8. pp. 339-347.
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    abstract = "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 {\AA} resolution in a binary complex with an NADP",
    author = "M. Fisher and J.T.M. Kroon and W. Martindale and A.R. Stuitje and A.R. Slabas and J.B. Rafferty",
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    language = "English",
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    The X-ray structure of Brassica napus ß-keto acyl carrier protein reductase and its implications for substrate binding and catalysis. / Fisher, M.; Kroon, J.T.M.; Martindale, W.; Stuitje, A.R.; Slabas, A.R.; Rafferty, J.B.

    In: Structure, Vol. 8, 2000, p. 339-347.

    Research output: Contribution to JournalArticleAcademicpeer-review

    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

    U2 - 10.1016/S0969-2126(00)00115-5

    DO - 10.1016/S0969-2126(00)00115-5

    M3 - Article

    VL - 8

    SP - 339

    EP - 347

    JO - Structure

    JF - Structure

    SN - 0969-2126

    ER -