ID Name Structure References (top 5) Molecular Target(s)
1ID:7132
D-CAMPHOR


NSC#:26351
Aldrich#:148075
Aldrich#:21293
Aldrich#:21295
Aldrich#:21300
Aldrich#:21310
Aldrich#:279676
Aldrich#:857300
Aldrich#:C352
Aldrich#:C6631
Aldrich#:C9380

Freqency:
in 1 ingredients:

  • 212
  • in 100 recipes:

  • 1
  • 3
  • 19
  • 29
  • 33
  • 41
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  • Properties
    C10H16O    152.24





    1:  Shimada H, Nagano S, Ariga Y, Unno M, Egawa T, Hishiki T, Ishimura Y, Masuya F, Obata T, Hori H.
    Putidaredoxin-cytochrome p450cam interaction. Spin state of the heme iron modulates putidaredoxin structure.
    J Biol Chem.    impact factor:   7.666
    1999;  274(14): 9363-9

    2:  Egawa T, Ogura T, Makino R, Ishimura Y, Kitagawa T.
    Observation of the O-O stretching Raman band for cytochrome P-450cam under catalytic conditions.
    J Biol Chem.    impact factor:   7.666
    1991;  266(16): 10246-8

    3:  Collins JR, Loew GH.
    Theoretical study of the product specificity in the hydroxylation of camphor, norcamphor, 5,5-difluorocamphor, and pericyclocamphanone by cytochrome P-450cam.
    J Biol Chem.    impact factor:   7.666
    1988;  263(7): 3164-70

    4:  Eble KS, Dawson JH.
    Novel reactivity of cytochrome P-450-CAM. Methyl hydroxylation of 5,5-difluorocamphor.
    J Biol Chem.    impact factor:   7.666
    1984;  259(23): 14389-93

    5:  Unno M, Ishimori K, Ishimura Y, Morishima I.
    High-pressure flash photolysis study of hemoprotein: effects of substrate analogues on the recombination of carbon monoxide to cytochrome P450CAM.
    Biochemistry.    impact factor:   4.493
    1994;  33(32): 9762-8

     
    Time used: 485 milliseconds.

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