400 18 Fatty Acid Hydroxylations using P450 Monooxygenases
Table 1.
Survey of P450 enzymes involved in fatty acid modification.
P450-family
Source
Expression system Chain-length
Hydroxylation position
References
terminal
subterminal
CYP2M1
rainbow trout liver COS-7 & insect cells C
12
x
-6
Yang et al., 1998
CYP4
Mammalian
only
x
-1
4Al
a
Rat, rabbit
Various
C
12
,C
14
,C
16
,C
20:4
Yes
2.5–50 %
Hoch et al., 2000
4A2
a
Rat
Various
C
12
,C
14
,C
20:4
Yes
14 –29 %
Hoch et al., 2000
4A3
a
Rat
Various
C
12
,C
14
,C
20:4
Yes
25 –45 %
Hoch et al., 2000
4A4
Rabbit
COS-1 cells
C
16
,C
20:4
Yes
<
20 %
Roman et al., 1993
4A5
Rabbit
Various
C
12
,C
16
,C
20
Yes
23 –42 %
Hosny et al., 1999
4A6
Rabbit
COS-1 cells
C
12
,C
16
,C
20:4
Yes
8 –27 %
Roman et al., 1993
4A7
Rabbit
Various
C
10
–C
22
Yes
6 –47 %
Sawamura et al., 1993
4A8
a
Rat
Various
C
12
,C
14
,C
16
Yes
40 –62 %
Hoch et al., 2000
4A11
a
Human
Various
C
12
,C
14
,C
16
Yes
5.9–45 %
Adas et al., 1999; Hoch et al., 2000
4B1
Human, rat, rabbit,mouse
Various
C
–C 8
10
,C
12
Yes
<
50 %
Fisher et al., 1998; Zheng etal., 1998
CYP52
Candida maltosa
A3
S. cerevisiae
C
12
,C
14
,C
16
Yes
Zimmer et al., 1996
A4
S. cerevisiae
C
12
,C
14
,C
16
Yes
Zimmer et al., 1996
A5
S. cerevisiae
C
12
,C
14
,C
16
Yes
<
5%,
x
-1
Zimmer et al., 1996
A9
S. cerevisiae
C
12
,C
14
,C
16
Yes
<
5%,
x
-1
Zimmer et al., 1996
A10
C. maltosa
CHA1 C
12
Yes
Zimmer et al., 1998a
A11
C. maltosa
CHA1 C
12
Yes
Zimmer et al., 1998a
CYP81B1
Helianthus tuberosus S. cerevisiae
WR,
WAT11, WAT21
C
10
,C
12
,C
14
x
-1,
x
-3,
x
-4 Cabello-Hurtado et al., 1998
CYP86A1
Arabidopsis thaliana S. cerevisiae
C
12
,C
14
,C
16
,C
18
Yes
Benveniste et al., 1998
CYP102
Bacillus megaterium
Various
E. coli
C
12
–C
22
Mutant F87A
x
-1,
x
-2,
x
-3 Boddupalli et al., 1990; Oliver
et al., 1997b
a
modified
N
-terminus and
C
-terminal His
-tag 6
