Biology Reference
In-Depth Information
ALA
ALA
ALA
ALA
10
11
12
0'
DV Proto
DV Proto
DV Proto
DV Proto
0'
12
13
DV Mg-Proto
DV Mg-Proto
DV Mg-Proto
DV Mg-Proto
10
11
DV Mpe
0'
12
4VMPR
13
DV Mpe
DV Mpe
DV Mpe
DV Pchlide
a
MV Mg-Proto
0'
POR-A
13
12
DV Pchlide
a
DV Pchlide
a
DV Chlide
a
MV Mpe
MV Mpe
4VPideR
10
4VPideR
11
4VCR
13
12
0'
M V Chlide a
M V Pchlide a
M V Pchlide a
MV Pchlide a
13
MV Pchlide
a
10
POR-B
11
15D
12
MV Chl a
POR-A
M V Chlide a
MV Pchlide b
4VPideR
14
0'
MV Chlide b
MV Chlide a
MV Chlide a
M V Chlide a
11
15D
10
12
0'
M V Chlide b
14
MV Chlide
a
E
MV Chl a
MV Chl a
MV Chl a
11
0'
12
10
MV Chl b
MV Chl b
MV Chl b
MV Chl b
MV Chl b
Fig. 7.12 Biosynthetic routes 10, 11, 0 0 and 13 which are responsible for the formation of DV
Mpe in LMV-DDV-LDMV plant species. Routes 10, 11, 0 0 and 13 are highlighted in green
(Adapted from Fig. 6.4 of Chap. 6 , and from Kolossov and Rebeiz 2010 )
source of enzyme, it is not possible to assign with certainty a precise mechanism for
its action without precise knowledge of the DV or MV nature of the Mpe substrate.
In Fig. 7.11 , three DV Mpe pools are depicted as being formed from DV Mg-Proto
via routes 1, 0 and 8. At this stage it is unclear whether the spatial biosynthetic
heterogeneity indicated by multiple resonance excitation energy transfer bands
(Table 6.1 ,Chap. 6 ) is accompanied by chemical biosynthetic heterogeneity or not. In
other words, it is unclear whether the biosynthesis of DV Mpe from DV Mg-Proto via
routes 1, 0 and 8 is catalyzed by identical SAMMTs or by SAMMT isozymes.
 
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