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4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
4-coumaroyl-CoA + NADPH + H+
4-coumaric aldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
caffeoyl-CoA + NADPH
caffeic aldehyde + CoA + NADP+
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
caffeoyl-CoA + NADPH + H+
caffeylaldehyde + CoA + NADP+
-
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffeylaldehyde + NADP+
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
coniferaldehyde + CoA + NADP+
feruloyl-CoA + NADPH + H+
-
-
-
-
r
coumaroyl-CoA + NADPH + H+
coumaraldehyde + CoA + NADP+
activity assay
-
-
?
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
feruloyl-CoA + NADPH
ferulic aldehyde + CoA + NADP+
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
p-coumaroyl-CoA + NADPH + H+
p-coumaraldehyde + CoA + NADP+
sinapaldehyde + CoA + NADP+
sinapoyl-CoA + NADPH + H+
-
-
-
-
r
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
additional information
?
-
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
low activity
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
chimeric 4CL1-CCR fusion enzyme
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
preferenced substrate
-
-
r
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
-
low activity
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
-
i.e. 4,5-dihydroxy-3-methoxycinnamoyl-CoA
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
-
i.e. 4,5-dihydroxy-3-methoxycinnamoyl-CoA
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
-
-
-
r
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH
caffeic aldehyde + CoA + NADP+
-
-
-
-
?
caffeoyl-CoA + NADPH
caffeic aldehyde + CoA + NADP+
-
poor substrate
-
?
caffeoyl-CoA + NADPH
caffeic aldehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
low activity
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
low activity
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
preferred substrate for isoform CCR2
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
chimeric 4CL1-CCR fusion enzyme
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
activity assay
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
preferenced substrate
-
-
r
caffeoyl-CoA + NADPH + H+
caffeylaldehyde + NADP+
-
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffeylaldehyde + NADP+
-
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffeylaldehyde + NADP+
-
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffeylaldehyde + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffeylaldehyde + NADP+
-
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffeylaldehyde + NADP+
-
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
Eucalyptus sp.
-
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
low activity
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
catalyzes preferentially the formation of cinnamaldehyde
catalyzes preferentially the formation of cinnamaldehyde
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
r
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
r
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
r
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
r
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
-
-
-
-
r
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
-
preferred substrate for isoform CCR2
-
-
?
feruloyl-CoA + NADPH
ferulic aldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH
ferulic aldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH
ferulic aldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH
ferulic aldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH
ferulic aldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH
ferulic aldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH
ferulic aldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
highly preferred substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
most favoured substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
preferred substrate for isoform CCR1
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate for isozyme CCR1
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
activity assay
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
highly specific for
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
chimeric 4CL1-CCR fusion enzyme
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate of isoform CCR1
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
activity assay
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate, which indicates preferential biosynthesis of G-type lignin
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
enzyme of lignification
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
enzyme of lignification
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
-
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
i.e. p-hydroxycinnamoyl-CoA, poor substrate
-
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
-
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
i.e. p-hydroxycinnamoyl-CoA, poor substrate
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
i.e. p-hydroxycinnamoyl-CoA, poor substrate
-
?
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
-
-
-
?
p-coumaroyl-CoA + NADPH + H+
p-coumaraldehyde + CoA + NADP+
-
-
-
-
?
p-coumaroyl-CoA + NADPH + H+
p-coumaraldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
-
low activity
-
?
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
very low efficiency
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
preferred substrate of isoform CCR2-1
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
activity assay
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
additional information
?
-
enzymatic assays with aGST-FaCCR reaction containing a mixture of equal molar amounts of three substrates (caffeoyl-, 4-coumaroyl-, and feruloyl-CoA), yield three major peaks that are identified as caffeic aldehyde (3,4-dihydroxycinnamaldehyde), 4-coumaraldehyde, and coniferaldehyde, respectively
-
-
?
additional information
?
-
-
enzymatic assays with aGST-FaCCR reaction containing a mixture of equal molar amounts of three substrates (caffeoyl-, 4-coumaroyl-, and feruloyl-CoA), yield three major peaks that are identified as caffeic aldehyde (3,4-dihydroxycinnamaldehyde), 4-coumaraldehyde, and coniferaldehyde, respectively
-
-
?
additional information
?
-
-
isozyme CCR1 also exhibits the highest turnover number with feruloyl-CoA and low activity with caffeoyl-CoA, while isozyme CCR2 prefers caffeoyl- and 4-coumaroyl-CoAs
-
-
?
additional information
?
-
isozyme CCR1 also exhibits the highest turnover number with feruloyl-CoA and low activity with caffeoyl-CoA, while isozyme CCR2 prefers caffeoyl- and 4-coumaroyl-CoAs
-
-
?
additional information
?
-
-
isozyme CCR2 also exhibits the highest turnover number with feruloyl-CoA and low activity with caffeoyl-CoA, while isozyme CCR2 prefers caffeoyl- and 4-coumaroyl-CoAs
-
-
?
additional information
?
-
isozyme CCR2 also exhibits the highest turnover number with feruloyl-CoA and low activity with caffeoyl-CoA, while isozyme CCR2 prefers caffeoyl- and 4-coumaroyl-CoAs
-
-
?
additional information
?
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
Ph-CCR1 is most active with feruloyl-CoA, followed by sinapoyl-CoA and 4-coumaroyl-CoA (relative to feruloyl-CoA, 65.4 and 21.6% activity, respectively), and only sparingly active with caffeoyl-CoA and benzoyl-CoA (below 1% activity). Ph-CCR1 exhibits the greatest catalytic efficiency (kcat/Km) with feruloyl-CoA and sinapoyl-CoA
-
-
?
additional information
?
-
-
Ph-CCR1 is most active with feruloyl-CoA, followed by sinapoyl-CoA and 4-coumaroyl-CoA (relative to feruloyl-CoA, 65.4 and 21.6% activity, respectively), and only sparingly active with caffeoyl-CoA and benzoyl-CoA (below 1% activity). Ph-CCR1 exhibits the greatest catalytic efficiency (kcat/Km) with feruloyl-CoA and sinapoyl-CoA
-
-
?
additional information
?
-
CCR converts hydroxycinnamoyl-CoA thioesters to their corresponding cinnamaldehydes in the presence of NADPH
-
-
?
additional information
?
-
isozyme PtoCCR1 exhibits specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. Substrate specificity, active site, molecular docking and modeling, overview
-
-
?
additional information
?
-
isozyme PtoCCR1 exhibits specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. Substrate specificity, active site, molecular docking and modeling, overview
-
-
?
additional information
?
-
-
isozyme PtoCCR1 exhibits specificity for feruloyl-CoA, with no detectable activity for any other hydroxycinnamoyl-CoA esters. Substrate specificity, active site, molecular docking and modeling, overview
-
-
?
additional information
?
-
no activity with sinapoyl-CoA by chimeric 4CL1-CCR fusion enzyme
-
-
?
additional information
?
-
substrate specificity, active site, molecular docking and modeling, overview. A132 in CCR7 combined with the catalytic triad might comprisethe catalytic center. In CCR7, L192, F155, and H208 are the substrate-binding sites
-
-
?
additional information
?
-
substrate specificity, active site, molecular docking and modeling, overview. A132 in CCR7 combined with the catalytic triad might comprisethe catalytic center. In CCR7, L192, F155, and H208 are the substrate-binding sites
-
-
?
additional information
?
-
-
substrate specificity, active site, molecular docking and modeling, overview. A132 in CCR7 combined with the catalytic triad might comprisethe catalytic center. In CCR7, L192, F155, and H208 are the substrate-binding sites
-
-
?
additional information
?
-
the substrates of CCR, cinnamoyl-CoA esters, are products of 4-coumarate-CoA ligase (4CL, EC 6.2.1.12), which is an enzyme upstream of CCR. Recombinant Pt4CL can catalyze the conversion of hydroxycinnamic acids to cinnamoyl-CoA esters, with high efficiency
-
-
?
additional information
?
-
although SbCCR1 displays higher affinity for caffeoyl-CoA or 4-coumaroyl-CoA than for feruloyl-CoA, the enzyme shows significantly higher activity for the latter substrate. Substrate specificity, molecular docking, overview. Thr154 of SbCCR1 and other CCRs likely confers strong substrate specificity for feruloyl-CoA over other cinnamoyl-CoA thioesters
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
4-coumaroyl-CoA + NADPH + H+
4-coumaric aldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
coniferaldehyde + CoA + NADP+
feruloyl-CoA + NADPH + H+
-
-
-
-
r
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
sinapaldehyde + CoA + NADP+
sinapoyl-CoA + NADPH + H+
-
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
additional information
?
-
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
-
-
-
r
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
preferenced substrate
-
-
r
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
-
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
preferred substrate for isoform CCR2
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
-
-
-
?
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
preferenced substrate
-
-
r
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
Eucalyptus sp.
-
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
r
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
r
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
r
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
r
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
-
-
-
-
?
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
-
-
-
-
r
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
-
preferred substrate for isoform CCR2
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
best substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
most favoured substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
preferred substrate for isoform CCR1
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
r
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
preferred substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
highly specific for
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
-
-
?
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
-
-
-
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
enzyme of lignification
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
-
-
?
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
-
enzyme of lignification
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
very low efficiency
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
?
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
-
-
-
-
?
additional information
?
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
-
based on its properties and expression pattern, PvCCR1 is probably associated with lignin biosynthesis during plant development and is therefore a target for the engineering of improved biomass, whereas PvCCR2 may function in defense
-
-
?
additional information
?
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
-
PvCCR1 is probably associated with lignin biosynthesis during plant development
-
-
?
additional information
?
-
CCR converts hydroxycinnamoyl-CoA thioesters to their corresponding cinnamaldehydes in the presence of NADPH
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0028 - 0.377
4-coumaroyl-CoA
0.0346 - 0.1824
5-hydroxyferuloyl-CoA
0.00516 - 0.617
caffeoyl-CoA
0.031 - 0.05
coniferaldehyde
0.06
coumaroyl-CoA
-
in 100 mM phosphate buffer pH 6.5, at 30°C
0.00042 - 0.323
feruloyl-CoA
0.00227 - 0.1
p-Coumaroyl-CoA
0.039 - 0.067
sinapaldehyde
0.00055 - 0.8769
sinapoyl-CoA
additional information
additional information
-
0.0028
4-coumaroyl-CoA
-
pH and temperature not specified in the publication
0.01595
4-coumaroyl-CoA
pH 6.0, 40°C, recombinant His-tagged wild-type enzyme
0.01636
4-coumaroyl-CoA
-
isoform CCR21, at pH 6.3 and 30°C
0.01973
4-coumaroyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.02408
4-coumaroyl-CoA
-
isoform CCR20, at pH 6.3 and 30°C
0.0248
4-coumaroyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
0.0316
4-coumaroyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.03666
4-coumaroyl-CoA
-
isoform CCR19, at pH 6.3 and 30°C
0.05581
4-coumaroyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.0572
4-coumaroyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.07
4-coumaroyl-CoA
pH 6.5, 30°C, mutant T154A
0.1
4-coumaroyl-CoA
pH 6.5, 30°C, wild-type enzyme
0.113
4-coumaroyl-CoA
pH 6.5, 30°C, mutant Y154Y
0.11608
4-coumaroyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.1165
4-coumaroyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.1265
4-coumaroyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.2086
4-coumaroyl-CoA
recombinant isozyme CCR1, pH 6.0, 25°C
0.2157
4-coumaroyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.2743
4-coumaroyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.377
4-coumaroyl-CoA
pH 6.25, 37°C, recombinant His-tagged enzyme
0.0346
5-hydroxyferuloyl-CoA
-
0.05
5-hydroxyferuloyl-CoA
-
-
0.099
5-hydroxyferuloyl-CoA
-
0.1824
5-hydroxyferuloyl-CoA
-
0.00516
caffeoyl-CoA
-
recombinant fusion protein GST-AtCCR2
0.0125
caffeoyl-CoA
-
recombinant fusion protein GST-AtCCR1
0.014
caffeoyl-CoA
pH 6.5, 30°C, wild-type enzyme
0.01885
caffeoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.02376
caffeoyl-CoA
pH 6.0, 40°C, recombinant His-tagged wild-type enzyme
0.0255
caffeoyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
0.0296
caffeoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.0376
caffeoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.04295
caffeoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.048
caffeoyl-CoA
-
in 100 mM phosphate buffer pH 6.5, at 30°C
0.09838
caffeoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.15233
caffeoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.1817
caffeoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.28301
caffeoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.3925
caffeoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.617
caffeoyl-CoA
pH 6.25, 37°C, recombinant His-tagged enzyme
0.031
coniferaldehyde
-
in 100 mM phosphate buffer pH 7.8, at 30°C
0.05
coniferaldehyde
-
in 100 mM phosphate buffer pH 6.5, at 30°C
0.00042
feruloyl-CoA
-
-
0.00098
feruloyl-CoA
-
recombinant fusion protein GST-AtCCR1
0.0027
feruloyl-CoA
-
isoform CCR21, at pH 6.3 and 30°C
0.0047
feruloyl-CoA
-
recombinant fusion protein GST-AtCCR2
0.00926
feruloyl-CoA
-
pH and temperature not specified in the publication
0.00986
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.01431
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged wild-type enzyme
0.01571
feruloyl-CoA
-
isoform CCR20, at pH 6.3 and 30°C
0.0161
feruloyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
0.01643
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A132T
0.01731
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A132S
0.0238
feruloyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.0254
feruloyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.02685
feruloyl-CoA
-
isoform CCR19, at pH 6.3 and 30°C
0.02759
feruloyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.03123
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155H
0.032
feruloyl-CoA
mutant enzyme S99G, pH and temperature not specified in the publication
0.0356
feruloyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.036
feruloyl-CoA
wild type enzyme, pH and temperature not specified in the publication
0.036
feruloyl-CoA
-
in 100 mM phosphate buffer pH 6.5, at 30°C
0.039
feruloyl-CoA
mutant enzyme L64W, pH and temperature not specified in the publication
0.042
feruloyl-CoA
mutant enzyme H215L, pH and temperature not specified in the publication
0.047
feruloyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.047
feruloyl-CoA
mutant enzyme R51G, pH and temperature not specified in the publication
0.04887
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A43V
0.057
feruloyl-CoA
mutant enzyme D77G, pH and temperature not specified in the publication
0.06
feruloyl-CoA
mutant enzyme V200E, pH and temperature not specified in the publication
0.063
feruloyl-CoA
pH 6.5, 30°C, mutant Y154Y
0.07
feruloyl-CoA
pH 6.5, 30°C, wild-type enzyme
0.07042
feruloyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.0716
feruloyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.07474
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant L192M
0.079
feruloyl-CoA
mutant enzyme S212G, pH and temperature not specified in the publication
0.0933
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.096
feruloyl-CoA
mutant enzyme F30V, pH and temperature not specified in the publication
0.102
feruloyl-CoA
mutant enzyme I31N, pH and temperature not specified in the publication
0.132
feruloyl-CoA
pH 6.5, 30°C, mutant Y310F
0.13699
feruloyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.155
feruloyl-CoA
pH 6.5, 30°C, mutant T154A
0.166
feruloyl-CoA
mutant enzyme R51G/D77G, pH and temperature not specified in the publication
0.244
feruloyl-CoA
mutant enzyme RF30V/I31N, pH and temperature not specified in the publication
0.3076
feruloyl-CoA
recombinant isozyme CCR1, pH 6.0, 25°C
0.323
feruloyl-CoA
pH 6.25, 37°C, recombinant His-tagged enzyme
0.0116
NADPH
-
cosubstrate sinapoyl-CoA
0.0143
NADPH
-
cosubstrate p-coumaroyl-CoA
0.0188
NADPH
-
cosubstrate feruloyl-CoA
0.028
NADPH
-
cosubstrate feruloyl-CoA
0.045
NADPH
-
cosubstrate feruloyl-CoA
0.12
NADPH
-
cosubstrate sinapoyl-CoA
0.29
NADPH
-
cosubstrate p-coumaroyl-CoA
0.00227
p-Coumaroyl-CoA
-
-
0.00427
p-Coumaroyl-CoA
-
-
0.039
sinapaldehyde
-
in 100 mM phosphate buffer pH 7.8, at 30°C
0.067
sinapaldehyde
-
in 100 mM phosphate buffer pH 6.5, at 30°C
0.00055
sinapoyl-CoA
-
-
0.00632
sinapoyl-CoA
-
recombinant fusion protein GST-AtCCR1
0.00658
sinapoyl-CoA
-
pH and temperature not specified in the publication
0.0102
sinapoyl-CoA
-
isoform CCR21, at pH 6.3 and 30°C
0.01924
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.02334
sinapoyl-CoA
-
isoform CCR20, at pH 6.3 and 30°C
0.0307
sinapoyl-CoA
-
recombinant fusion protein GST-AtCCR2
0.03494
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A43V
0.04102
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged wild-type enzyme
0.05092
sinapoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.0548
sinapoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.0565
sinapoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.057
sinapoyl-CoA
-
in 100 mM phosphate buffer pH 6.5, at 30°C
0.06254
sinapoyl-CoA
-
isoform CCR19, at pH 6.3 and 30°C
0.0766
sinapoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.078
sinapoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.1533
sinapoyl-CoA
-
at pH 6.0, temperature not specified in the publication
0.2703
sinapoyl-CoA
recombinant isozyme CCR1, pH 6.0, 25°C
0.56836
sinapoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.8769
sinapoyl-CoA
-
at pH 6.0, temperature not specified in the publication
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics analysis
-
additional information
additional information
thermodynamics and Michaelis-Menten kinetics
-
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0.0000265 - 8.42
4-coumaroyl-CoA
4.9
5-hydroxyferuloyl-CoA
-
0.0000293 - 113
caffeoyl-CoA
0.00234 - 164
feruloyl-CoA
0.0000265
4-coumaroyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
0.0142
4-coumaroyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.0183
4-coumaroyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.019
4-coumaroyl-CoA
-
isoform CCR21, at pH 6.3 and 30°C
0.02
4-coumaroyl-CoA
pH 6.5, 30°C, mutant T154A
0.031
4-coumaroyl-CoA
mutant S123T of isoform CCR1, pH and temperature not specified in the publication
0.05
4-coumaroyl-CoA
pH 6.5, 30°C, wild-type enzyme
0.129
4-coumaroyl-CoA
-
isoform CCR20, at pH 6.3 and 30°C
0.188
4-coumaroyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.232
4-coumaroyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.32
4-coumaroyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.324
4-coumaroyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.353
4-coumaroyl-CoA
-
isoform CCR19, at pH 6.3 and 30°C
1.2
4-coumaroyl-CoA
recombinant isozyme CCR1, pH 6.0, 25°C
8.42
4-coumaroyl-CoA
pH 6.5, 30°C, mutant Y154Y
0.0000293
caffeoyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
0.01
caffeoyl-CoA
pH 6.5, 30°C, wild-type enzyme
0.0145
caffeoyl-CoA
-
recombinant fusion protein GST-AtCCR2
0.0327
caffeoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.0362
caffeoyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.0363
caffeoyl-CoA
-
recombinant fusion protein GST-AtCCR1
0.093
caffeoyl-CoA
mutant S123T of isoform CCR1, pH and temperature not specified in the publication
0.162
caffeoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.23
caffeoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.326
caffeoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.559
caffeoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
113
caffeoyl-CoA
-
in 100 mM phosphate buffer pH 6.5, at 30°C
94
coniferaldehyde
-
in 100 mM phosphate buffer pH 6.5, at 30°C
236
coniferaldehyde
-
in 100 mM phosphate buffer pH 7.8, at 30°C
0.43
coumaroyl-CoA
CCR1
105
coumaroyl-CoA
-
in 100 mM phosphate buffer pH 6.5, at 30°C
0.00234
feruloyl-CoA
pH 6.0, 25°C, recombinant GST-tagged enzyme
0.0101
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A132T
0.0192
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A132S
0.027
feruloyl-CoA
-
isoform CCR21, at pH 6.3 and 30°C
0.0372
feruloyl-CoA
-
recombinant fusion protein GST-AtCCR2
0.038
feruloyl-CoA
-
recombinant fusion protein GST-AtCCR1
0.063
feruloyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.136
feruloyl-CoA
mutant S123T of isoform CCR1, pH and temperature not specified in the publication
0.1409
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155H
0.18
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.191
feruloyl-CoA
-
isoform CCR19, at pH 6.3 and 30°C
0.24
feruloyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.289
feruloyl-CoA
isoform CCR1, pH and temperature not specified in the publication
0.377
feruloyl-CoA
-
isoform CCR20, at pH 6.3 and 30°C
0.47
feruloyl-CoA
pH 6.5, 30°C, mutant Y310F
0.74
feruloyl-CoA
pH 6.5, 30°C, mutant T154A
0.8375
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A43V
1.033
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
1.905
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant L192M
2.01
feruloyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
2.1
feruloyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
3.96
feruloyl-CoA
pH 6.5, 30°C, wild-type enzyme
5.8
feruloyl-CoA
recombinant isozyme CCR1, pH 6.0, 25°C
17.24
feruloyl-CoA
pH 6.5, 30°C, mutant Y154Y
24
feruloyl-CoA
mutant enzyme S212G, pH and temperature not specified in the publication
44
feruloyl-CoA
mutant enzyme H215L, pH and temperature not specified in the publication
84
feruloyl-CoA
mutant enzyme R51G/D77G, pH and temperature not specified in the publication
100
feruloyl-CoA
mutant enzyme R51G, pH and temperature not specified in the publication
108
feruloyl-CoA
mutant enzyme D77G, pH and temperature not specified in the publication
122
feruloyl-CoA
mutant enzyme V200E, pH and temperature not specified in the publication
137
feruloyl-CoA
mutant enzyme F30V, pH and temperature not specified in the publication
142
feruloyl-CoA
mutant enzyme RF30V/I31N, pH and temperature not specified in the publication
144
feruloyl-CoA
mutant enzyme S99G, pH and temperature not specified in the publication
155
feruloyl-CoA
mutant enzyme I31N, pH and temperature not specified in the publication
160
feruloyl-CoA
mutant enzyme L64W, pH and temperature not specified in the publication
162
feruloyl-CoA
wild type enzyme, pH and temperature not specified in the publication
164
feruloyl-CoA
-
in 100 mM phosphate buffer pH 6.5, at 30°C
81
sinapaldehyde
-
in 100 mM phosphate buffer pH 6.5, at 30°C
210
sinapaldehyde
-
in 100 mM phosphate buffer pH 7.8, at 30°C
0.012
sinapoyl-CoA
-
isoform CCR21, at pH 6.3 and 30°C
0.013
sinapoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.052
sinapoyl-CoA
mutant S123T of isoform CCR1, pH and temperature not specified in the publication
0.0583
sinapoyl-CoA
-
recombinant fusion protein GST-AtCCR2
0.0612
sinapoyl-CoA
-
recombinant fusion protein GST-AtCCR1
0.064
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged enzyme
0.094
sinapoyl-CoA
-
isoform CCR20, at pH 6.3 and 30°C
0.098
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant A43V
0.135
sinapoyl-CoA
pH 6.0, 40°C, recombinant His-tagged mutant F155Y
0.2
sinapoyl-CoA
100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH
0.261
sinapoyl-CoA
isoform CCR2-1, pH and temperature not specified in the publication
0.57
sinapoyl-CoA
-
isoform CCR19, at pH 6.3 and 30°C
0.829
sinapoyl-CoA
isoform CCR1, pH and temperature not specified in the publication
3.4
sinapoyl-CoA
recombinant isozyme CCR1, pH 6.0, 25°C
131
sinapoyl-CoA
-
in 100 mM phosphate buffer pH 6.5, at 30°C
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evolution
phylogenetic analysis shows that HcCCR1 is more closely related to HcCCR2 and Arabidopsis thaliana AtCCR proteins than CCR-like proteins. HcCCR1 and HcCCR2 are encoded onto two different genes
evolution
the conserved motifs G-X-X-G-X-X-A and D-X-X-D are reported to be involved in NAD(P) binding and adenine binding pocket stabilization. In addition, the NADP specificity motif R(X)5K is identified, which is a key structure that distinguishes CCR from other NAD(H)-dependent SDRs. Sequence comparisons and phylogenetic analysis of Populus tometosa CCRs, overview. Of the 11 PtoCCR and PtoCCR-like proteins, PtoCCR1 and 7 each catalyze at least one substrate. PtoCCR1 is active only with feruloyl-CoA as a substrate, while PtoCCR7 accepts all hydroxycinnamoyl-CoA esters
evolution
-
phylogenetic analysis shows that HcCCR1 is more closely related to HcCCR2 and Arabidopsis thaliana AtCCR proteins than CCR-like proteins. HcCCR1 and HcCCR2 are encoded onto two different genes
-
malfunction
-
Ccr1 knockout mutants exhibit a dramatic decrease in S lignin in vascular tissue
malfunction
-
in the ccr1 mutant, CCR1 gene expression is reduced to 31% of the residual wild type level leading to a decrease in lignin content and significant changes in lignin structure. 4-hydroxyphenyl units are strongly decreased and the syringyl/guaiacyl ratio is slightly increased. Down-regulation of CCR1 alters schlerenchymatic fibre morphology and cell wall structure. Moderate down-regulation of CCR1 significantly improves cell wall digestibility in maize
malfunction
-
20 month-old trees transgenic trees with downregulated CCR enzymes show up to 161% increased ethanol yield from tissues including bark, generated from the lignocellulosic biomass, strong downregulation of CCR also affects biomass yield. Wood samples derived from the transgenic trees are more easily processed into ethanol than wild-type. The improved saccharification yield is due to a higher cellulose conversion and correlates with the abundance of ferulic acid markers
malfunction
AtCCR2 expression is increased in Arabidopsis ccr1 mutant and function is partly compensated
malfunction
Betula platyphylla x Betula pendula
BpCCR1 overexpression increases lignin content up to 14.6%, and its suppression decreases lignin content by 6.3%. Modification of BpCCR1 expression leads to conspicuous changes in wood characteristics, including xylem vessel number and arrangement, and secondary wall thickness. The growth of transgenic trees in terms of height is also significantly influenced by the modification of BpCCR1 genes. The secondary xylem microstructures of stems base is altered with thicker cell walls of xylem fibers, penotype, overview
malfunction
-
ccr1 mutants exhibits multiple abnormalities, including increased cell proliferation. The ccr1 phenotypes are not due to the reduced lignin content, but instead are due to the dramatically increased level of ferulic acid (FeA), an intermediate in lignin biosynthesis. The levels of reactive oxygen species (ROS) in ccr1 are markedly reduced. Reduced ferulic acid levels in plants result in an increase in ROS levels and defective cell proliferation
malfunction
levels of G-monomers are considerably reduced in FaCCR-silenced fruits. Phenotypic analysis shows that the texture of the fruits injected with different FaCCR constructs is more solid than that of the untreated fruits , but up- or downregulation of the enzyme does not alter the red color and appearance of the fruits
malfunction
T154Y mutation in SbCCR1 leads to broader substrate specificity and faster turnover
malfunction
the positively charged extended structure of His208 was important in stabilizing CoA, while the mutants (M208, V208, and Y208) were unable to assume this function
malfunction
-
enzyme downregulation increases the biosynthesis of phenolic acids
malfunction
-
enzyme knockdown transgenics display a decrease in root and anther lignin depositions. Isoform CCR14 knockdown transgenics display loss of lignification in their anthers
malfunction
-
suppression of enzyme gene expression results in a reduction in cinnamyl alcohol dehydrogenase enzyme activity in stem-differentiating xylem
malfunction
truncated enzyme lines (CCR-3, CCR-7 and CCR-12) show marked reduction in guaiacyl lignin which is reduced by 10.2% in both CCR-3 and CCR-7, and 9.3% in CCR-12. The down-regulation of lignin leads to significant increase in total phenolics content than the wild type control
malfunction
-
ccr1 mutants exhibits multiple abnormalities, including increased cell proliferation. The ccr1 phenotypes are not due to the reduced lignin content, but instead are due to the dramatically increased level of ferulic acid (FeA), an intermediate in lignin biosynthesis. The levels of reactive oxygen species (ROS) in ccr1 are markedly reduced. Reduced ferulic acid levels in plants result in an increase in ROS levels and defective cell proliferation
-
metabolism
the enzyme carries out the first committed step in monolignol biosynthesis and acts as a first regulatory point in lignin formation
metabolism
cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis
metabolism
cinnamoyl-CoA reductase (CCR) is the first enzyme in the monolignol-specific branch of the lignin biosynthetic pathway
metabolism
cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis. It is likely that Mt-CCR1 is the major CCR isozyme involved in lignin biosynthesis, and Mt-CCR2 is proposed to be involved in an alternative route for S lignin biosynthesis in Medicago truncatula
metabolism
-
enzyme cinnamoyl-CoA reductase (CCR) catalyzes the first step in the monolignol-specific branch of the lignin biosynthetic pathway
metabolism
Betula platyphylla x Betula pendula
the enzyme is a key enzyme involved in the lignin biosynthesis pathway
metabolism
the enzyme is involved in lignin biosynthesis
metabolism
the enzyme is involved in the lignin biosynthesis pathway
metabolism
the enzyme is involved in the Monolignol biosynthetic pathway in dicotyledonous angiosperms, pathway overview
metabolism
the enzyme is involved in the the monolignol biosynthetic pathway
metabolism
the formation of 4-hydroxycinnamaldehydes is catalyzed by 4-coumaric acid:coenzyme A ligase (4CL1) and cinnamoyl coenzyme A reductase (CCR). 4-Hydroxycinnamaldehydes are a class of natural plant secondary products that includes coniferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffealdehyde. They are involved in several secondary metabolism pathways, such as those involved in the biosynthesis of phenolic acids, monolignols, flavonoids and terpenoids. 4-Hydroxycinnamaldehydes are also key intermediates in the biosynthesis and degradation of lignins, which protect cell wall polysaccharides from microbial degradation
metabolism
rain shelter treatment may affect phenylalanine lignin monomer synthesis and subsequent cork accumulation by altering the expression or enzyme activities of phenylalanine ammonia lyase (PAL), catechol-O-methyltransferase (COMT), cinnamoyl-CoA reductase (CCR), cinnamyl alcohol dehydrogenase (CAD), peroxidase (POD), and omega-hydroxypalmitate O-feruloyl transferase (HHT1), thus decreasing exocarp russet accumulation in semi-russet pear
metabolism
-
cinnamoyl CoA reductase is the dedicated enzyme in the lignin pathway
metabolism
-
isoform CCR14 is a substrate of the SCF(FBK1) E3 ligase complex, and its degradation is mediated by the 26S proteasome
physiological function
CCR is responsible for the CoA ester conversion into aldehyde in monolignol biosynthesis, which diverts phenylpropanoid-derived metabolites into the biosynthesis of lignin. Lignifications in blueberry fruits are regulated under various post-harvest conditions
physiological function
-
cinnamoyl CoA reductase 1 (CCR1) is a key factor involved in progressive exit from the cell proliferation phase. CCR1 catalyzes the NADPH-dependent reduction of cinnamoyl CoA esters to their corresponding cinnamaldehydes, an important step in the biosynthesis of lignin monomers. Enzyme CCR1, ferulic acid, and reactive oxygen species coordinate cell proliferation exit in normal leaf development. Ferulic acid is known to have antioxidant activity. CCR1 acts through depletion of feruclic acid to coordinate with ROS to direct exit from the cell proliferation phase during leaf development
physiological function
cinnamoyl-CoA reductase catalyzes the reduction of cinnamoyl-CoA esters to their respective cinnamaldehydes and is considered as a key enzyme in lignin formation
physiological function
cinnamoyl-coenzyme A reductase (CCR) catalyzes the reduction of hydroxycinnamoyl-CoA esters using NADPH to produce hydroxycinnamyl aldehyde precursors in lignin synthesis. Isozyme SbCCR2 displays greater activity toward 4-coumaroyl-CoA than does isozyme SbCCR1, which implies a role in the synthesis of defense-related lignin. CCR1 is involved in lignification of stem tissues, whereas CCR2 is involved in lignification in response to attack by pathogens
physiological function
-
enzyme CCR is involved in lignin biosynthesis and might be playing a role in drought and salinity stress
physiological function
Betula platyphylla x Betula pendula
specific functions of a birch enzyme CCR1 in wood formation and growth
physiological function
the enzyme is involved in drought defense
physiological function
-
isoform CCR20 is primarily involved in developmental deposition of lignins in secondary cell walls
physiological function
-
vessel-specific reintroduction of isoform CCR1 in dwarfed ccr1 mutants restores vessel and xylary fiber integrity and increases biomass
physiological function
-
cinnamoyl CoA reductase 1 (CCR1) is a key factor involved in progressive exit from the cell proliferation phase. CCR1 catalyzes the NADPH-dependent reduction of cinnamoyl CoA esters to their corresponding cinnamaldehydes, an important step in the biosynthesis of lignin monomers. Enzyme CCR1, ferulic acid, and reactive oxygen species coordinate cell proliferation exit in normal leaf development. Ferulic acid is known to have antioxidant activity. CCR1 acts through depletion of feruclic acid to coordinate with ROS to direct exit from the cell proliferation phase during leaf development
-
additional information
active site characterization of Ll-CCRH1 by modeling/docking, site directed mutagenesis and chemical modification studies, conformational transitions of Ll-CCRH1 are studied using fluorescence and circualar dichroism spectroscopy, overview. Native Ll-CCRH1 is a multi tryptophan protein, the active site of Ll-CCRH1 is made up of 10 residues, that is, Phe30, Ile31, Arg51, Asp77, Ser136, Tyr170, Lys174, Val200, Ser212, and His215
additional information
-
active site characterization of Ll-CCRH1 by modeling/docking, site directed mutagenesis and chemical modification studies, conformational transitions of Ll-CCRH1 are studied using fluorescence and circualar dichroism spectroscopy, overview. Native Ll-CCRH1 is a multi tryptophan protein, the active site of Ll-CCRH1 is made up of 10 residues, that is, Phe30, Ile31, Arg51, Asp77, Ser136, Tyr170, Lys174, Val200, Ser212, and His215
additional information
-
structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview
additional information
structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview
additional information
structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview. The location of the nicotinamide ring in Ph-CCR1, at the end of a deep cleft, consequently dictates that the hydroxycinnamoyl-CoA substrate is bound with a U-shaped conformation and mostly likely with the phenylpropenyl moiety accommodated within the deepest part of the cleft and the CoA portion folded over and occupying the cleft's outer region. The Ph-CCR1 binding pocket for the phenolic ring is formed by several aliphatic side chains (Ile124, Gly125, Val185, Leu186, and Ala220) and is capped by Tyr284, which is suitably positioned to form a hydrogen bond with the substrate's phenolic (C4) hydroxyl group, importance for CCR of interactions with the 4-hydroxyl group of the ligand's phenolic ring. Substrate binding structure, overview
additional information
-
structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview. The location of the nicotinamide ring in Ph-CCR1, at the end of a deep cleft, consequently dictates that the hydroxycinnamoyl-CoA substrate is bound with a U-shaped conformation and mostly likely with the phenylpropenyl moiety accommodated within the deepest part of the cleft and the CoA portion folded over and occupying the cleft's outer region. The Ph-CCR1 binding pocket for the phenolic ring is formed by several aliphatic side chains (Ile124, Gly125, Val185, Leu186, and Ala220) and is capped by Tyr284, which is suitably positioned to form a hydrogen bond with the substrate's phenolic (C4) hydroxyl group, importance for CCR of interactions with the 4-hydroxyl group of the ligand's phenolic ring. Substrate binding structure, overview
additional information
the HcCCR1 protein contains a conserved NWYCYGK catalytic domain at the N-terminal region of the HcCCR1 protein
additional information
the substrate-binding domain of the SbCCR1 is surrounded by two groups of a-helices, and the floor of the substrate-binding pocket is largely composed of beta-strands. Residues T154 and Y310 ae involved in substrate binding with ferulic acid, Tyr310 binds the 4-hydroxyl of feruloyl-CoA, while Thr154 binds the 3-methoxy group of this molecule. Molecular docking and modelling, overview
additional information
three-dimensional structure analysis of wild-type and mutant enzymes, molecular docking and modeling, overview
additional information
three-dimensional structure analysis of wild-type and mutant enzymes, molecular docking and modeling, overview
additional information
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three-dimensional structure analysis of wild-type and mutant enzymes, molecular docking and modeling, overview
additional information
three-dimensional structure analysis, molecular docking and modeling, overview
additional information
three-dimensional structure analysis, molecular docking and modeling, overview
additional information
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three-dimensional structure analysis, molecular docking and modeling, overview
additional information
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the HcCCR1 protein contains a conserved NWYCYGK catalytic domain at the N-terminal region of the HcCCR1 protein
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D77A
the mutant shows specificity towards coumaroyl-CoA
D77N
the mutant has same substrate affinity (feruloyl CoA) as that of wild type enzyme
F30L
the mutant shows preference for coumaroyl-CoA
F30S
the mutant shows preference for coumaroyl-CoA
F30V/I31N
the mutant shows approximately 7fold increase in Km and 8fold decrease in kcat/Km values
F30Y
the mutant shows preference for coumaroyl-CoA
H215R
coumaroyl-CoA is specific for mutant H215R
H215Y
5-hydroxyferuloyl-CoA is specific for mutant H215Y
I131N
the mutant shows slightly reduced catalytic efficiency compared to the wild type
I31F
the mutant shows more negative binding energy for hydroxyferuloyl CoA
I31M
the mutant exhibits equal affinity for coumaroyl and hydroxyferulol CoA
K174E
the mutant shows coumaroyl-CoA as preferred substrate
K174N
the mutant has favorable binding energy for hydroxyferuloyl-CoA
K174R
the mutant has favorable binding energy for hydroxyferuloyl-CoA
K174T
the mutant shows coumaroyl-CoA as preferred substrate
L64W
the mutant shows no significant change in Km values compared to the wild type enzyme
R51G/D77G
the mutant displays 5fold increase in Km and around 9fold reduction in specificity constant
R51K
the mutant shows affinity towards caffeoyl-CoA
S136C
coumaroyl CoA is a better substrate for mutant S136C
S136P
the mutant shows favored specificity for feruloyl-CoA
S136T
the mutant shows favored specificity for feruloyl-CoA
S136Y
the mutant shows preference for caffeoyl-CoA
S212T
the mutant shows feruloyl CoA as promising substrate
S99G
the mutant shows no significant change in Km values compared to the wild type enzyme
V200A
the mutant displays substrate specificity towards coumaroyl-CoA
V200G
the mutant displays substrate specificity towards coumaroyl-CoA
V200M
the mutant exhibits increased affinity for coumaroyl-CoA
Y170C
the mutant displays less number of interactions compared to the wild type enzyme
Y170F
the mutant shows preference for coumaroyl-CoA
Y170N
the mutant shows preference for coumaroyl-CoA
A132S
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
A132T
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
A43V
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
F155H
site-directed mutagenesis, the mutant is only active with feruloyl-CoA as substrate in contrast to the wild-type enzyme
F155Y
site-directed mutagenesis, the mutant exhibits greater catalytic efficiency for sinapoyl-CoA compared to the wild-type PtoCCR7
H208M
site-directed mutagenesis, inactive mutant
H208V
site-directed mutagenesis, inactive mutant
H208Y
site-directed mutagenesis, inactive mutant
L192M
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
S123T
the mutant shows reduced activity compared to the wild type enzyme
T154A
the mutant enzyme displays significantly lower affinity for feruloyl-CoA compared with the wild-type enzyme
T154Y
the mutation in SbCCR1 leads to broader substrate specificity and faster turnover. The T154Y mutant exhibits 4.9 and 144fold increases in catalytic efficiency for feruloyl-CoA and 4-coumaroyl-CoA, respectively, over those of wild-type SbCCR1
Y310F
the mutant enzyme displays significantly lower affinity for feruloyl-CoA compared with the wild-type enzyme
D77G
site-directed mutagenesis, structure comparison to the wild-type enzyme
D77G
the mutant displays equal affinity for caffeoyl-CoA and sinapoyl-CoA
D77G
the mutant displays higher Km values (up to 4fold), indicating lower affinity toward substrate, while catalytic efficiencies for these mutant is notably decreased
F30V
site-directed mutagenesis, structure comparison to the wild-type enzyme
F30V
the mutant displays higher Km values (up to 4fold), indicating lower affinity toward substrate, while catalytic efficiencies for these mutant is notably decreased
F30V
the mutant prefers feruloyl-CoA as favoured substrate
H215L
site-directed mutagenesis, structure comparison to the wild-type enzyme
H215L
the mutant displays preference for sinapoyl-CoA
H215L
the mutant shows no significant change in Km values compared to the wild type enzyme
I31N
site-directed mutagenesis, structure comparison to the wild-type enzyme
I31N
the mutant demonstrates better affinity for sinapoyl CoA over others
K174M
site-directed mutagenesis, structure comparison to the wild-type enzyme
K174M
the mutant is specific for feruloyl CoA
K174M
the mutant shows complete loss of activity with feruloyl-CoA as substrate
R51G
site-directed mutagenesis, structure comparison to the wild-type enzyme
R51G
the mutant displays higher Km values (up to 4fold), indicating lower affinity toward substrate, while catalytic efficiencies for these mutant is notably decreased
R51G
the mutation alters side chain from polar charged to small compact neutral residue, resulting in marked decrease in accessible surface area and leads to loss of interactions with substrate
S136A
site-directed mutagenesis, structure comparison to the wild-type enzyme
S136A
coumaroyl CoA is a better substrate for mutant S136A
S136A
the mutant shows complete loss of activity with feruloyl-CoA as substrate
S212G
site-directed mutagenesis, structure comparison to the wild-type enzyme
S212G
the mutant exhibits the catalytic efficiencies less than 10% of wild type enzyme
S212G
the mutant shows a 2.5fold increase in Km, 7fold reduction in kcat and 15fold decrease in kcat/Km
V200E
site-directed mutagenesis, structure comparison to the wild-type enzyme
V200E
the mutant shows reduced catalytic efficiency compared to the wild type
Y170H
site-directed mutagenesis, structure comparison to the wild-type enzyme
Y170H
the mutant demonstrates affinity for feruloyl-CoA
Y170H
the mutant shows complete loss of activity with feruloyl-CoA as substrate
additional information
in CCR-deficient plants, valuable marker compound is present in lignins, which derivates from novel structures produced when ferulic acid is incorporated into lignins
additional information
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two knockout mutants for CCR1. Both have a dwarf phenotype and a delayed senescence. At complete maturity, their inflorescence stems display a 25-35% decreased lignin level, some alterations in lignin structure with a higher frequency of resistant interunit bonds and a higher content in cell wall-bound ferulic esters. Ferulic acid-coniferyl alcohol ether dimers in cell walls show similar levels in wild-type and mutant plants. Expression of CCR2, involved in plant defense, is increased in the mutants and can account for the biosynthesis of lignins in the CCR1-knockout plants. CCR1-mutant plantlets have 3 to 4times less sinapoyl malate than controls and accumulate some feruloyl malate. The same compositional changes occurr in the rosette leaves of greenhouse-grown plants. Relative to the control, stems accumulate unusually high levels of both sinapoyl malate and feruloyl malate as well as more kaempferol glycoside
additional information
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identification and analysis of Arabidopsis thaliana mutant 'asymmetric leaves1/2 enhancer7' (ae7), which shows defective cell proliferation, ae7 has reduced numbers of cells in the leaf and root, Gene CCR1 in this mutant carries a C to T substitution in the third exon, resulting in an amino acid change from serine to phenylalanine. Mutational modification and analysis, phenotypes, overview
additional information
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identification and analysis of Arabidopsis thaliana mutant 'asymmetric leaves1/2 enhancer7' (ae7), which shows defective cell proliferation, ae7 has reduced numbers of cells in the leaf and root, Gene CCR1 in this mutant carries a C to T substitution in the third exon, resulting in an amino acid change from serine to phenylalanine. Mutational modification and analysis, phenotypes, overview
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additional information
Betula platyphylla x Betula pendula
construction of enzyme overexpression and suppression lines, vector transfection using Agrobacterium tumefaciens strain EHA105
additional information
gene expression level and enzymatic activity of FaCCR are efficiently suppressed through RNAi in FaCCR-silenced strawberries. Levels of G-monomers are considerably reduced in FaCCR-silenced fruits. The ihpRNA-FaCCR construct shows sequence-specific interference with homolo-gous FaCCR expression in the fruits, phenotype, overview
additional information
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gene expression level and enzymatic activity of FaCCR are efficiently suppressed through RNAi in FaCCR-silenced strawberries. Levels of G-monomers are considerably reduced in FaCCR-silenced fruits. The ihpRNA-FaCCR construct shows sequence-specific interference with homolo-gous FaCCR expression in the fruits, phenotype, overview
additional information
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in CCR-deficient plants, valuable marker compound is present in lignins, which derivates from novel structures produced when ferulic acid is incorporated into lignins
additional information
4-coumaric acid:coenzyme A ligase (4CL1) and cinnamoyl coenzyme A reductase (CCR) are fused by means of genetic engineering to generate an artificial bifunctional enzyme. Chimeric 4CL1-CCR is overexpressed in Escherichia coli supplemented with phenylpropanoic acids. Three 4-hydroxycinnamaldehydes, p-coumaraldehyde, caffealdehyde and coniferaldehyde, are thereby biosynthesized and secreted into the culture medium. Extracellular hydroxycinnamoyl-CoA thioesters are not detected, hydroxycinnamoyl-CoA thioesters accumulate only in the cell, because they cannot freely pass through the cellular membrane. The fusion enzyme 4CL1-CCR can catalyze sequential multistep reactions, thereby avoiding the permeability problem of intermediates, which reveals its superiority over a mixture of individual native enzymes. The bifunctional enzyme 4CL1-CCR plays a central role in cellular metabolism by converting phenylpropanoic acids to their corresponding cinnamaldehydes
additional information
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construction of genetically modified poplars, that are downregulated for cinnamoyl-CoA reductase (CCR). 20 month-old trees transgenic trees with downregulated CCR enzymes show up to 161% increased ethanol yield from tissues including bark, generated from the lignocellulosic biomass, strong downregulation of CCR also affects biomass yield. Wood samples derived from the transgenic trees are more easily processed into ethanol than wild-type
additional information
in CCR-deficient poplar, valuable marker compound is present in lignins, which derivates from novel structures produced when ferulic acid is incorporated into lignins
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Li, J.; Fan, F.; Wang, L.; Zhan, Q.; Wu, P.; Du, J.; Yang, X.; Liu, Y.
Cloning and expression analysis of cinnamoyl-CoA reductase (CCR) genes in sorghum
PeerJ
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2016
Sorghum bicolor, Sorghum bicolor (C5XWV7), Sorghum bicolor (C5YLL4)
brenda
Srivastava, S.; Vishwakarma, R.K.; Arafat, Y.A.; Gupta, S.K.; Khan, B.M.
Abiotic stress induces change in cinnamoyl CoA reductase (CCR) protein abundance and lignin deposition in developing seedlings of Leucaena leucocephala
Physiol. Mol. Biol. Plants
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197-205
2015
Leucaena leucocephala
brenda
Zhang, W.; Wei, R.; Chen, S.; Jiang, J.; Li, H.; Huang, H.; Yang, G.; Wang, S.; Wei, H.; Liu, G.
Functional characterization of CCR in birch (Betula platyphylla x Betula pendula) through overexpression and suppression analysis
Physiol. Plant.
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2015
Betula platyphylla x Betula pendula (G3FJ91)
brenda
Pan, H.; Zhou, R.; Louie, G.V.; Muehlemann, J.K.; Bomati, E.K.; Bowman, M.E.; Dudareva, N.; Dixon, R.A.; Noel, J.P.; Wang, X.
Structural studies of cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase, key enzymes of monolignol biosynthesis
Plant Cell
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3709-3727
2014
Medicago truncatula, Medicago truncatula (G7JEE5), Petunia x hybrida (A0A059TC02), Petunia x hybrida
brenda
Xue, J.; Luo, D.; Xu, D.; Zeng, M.; Cui, X.; Li, L.; Huang, H.
CCR1, an enzyme required for lignin biosynthesis in Arabidopsis, mediates cell proliferation exit for leaf development
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2015
Arabidopsis thaliana, Arabidopsis thaliana Col-0
brenda
Sattler, S.A.; Walker, A.M.; Vermerris, W.; Sattler, S.E.; Kang, C.
Structural and biochemical characterization of cinnamoyl-CoA reductases
Plant Physiol.
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2017
Sorghum bicolor (C5YLL4)
brenda
Chao, N.; Li, N.; Qi, Q.; Li, S.; Lv, T.; Jiang, X.N.; Gai, Y.
Characterization of the cinnamoyl-CoA reductase (CCR) gene family in Populus tomentosa reveals the enzymatic active sites and evolution of CCR
Planta
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61-75
2017
Populus tomentosa (A0A0F7EVN0), Populus tomentosa (T1WWB5), Populus tomentosa
brenda
Van Acker, R.; Leple, J.C.; Aerts, D.; Storme, V.; Goeminne, G.; Ivens, B.; Legee, F.; Lapierre, C.; Piens, K.; Van Montagu, M.C.; Santoro, N.; Foster, C.E.; Ralph, J.; Soetaert, W.; Pilate, G.; Boerjan, W.
Improved saccharification and ethanol yield from field-grown transgenic poplar deficient in cinnamoyl-CoA reductase
Proc. Natl. Acad. Sci. USA
111
845-850
2014
Populus tremula x Populus alba
brenda
Ghosh, R.; Choi, B.; Cho, B.K.; Lim, H.S.; Park, S.U.; Bae, H.J.; Natarajan, S.; Bae, H.
Characterization of developmental- and stress-mediated expression of cinnamoyl-CoA reductase in kenaf (Hibiscus cannabinus L.)
ScientificWorldJournal
2014
601845
2014
Hibiscus cannabinus (A0A023HHB5), Hibiscus cannabinus (D9ZKR8), Hibiscus cannabinus
brenda
Ponniah, S.; Shang, Z.; Akbudak, M.; Srivastava, V.; Manoharan, M.
Down-regulation of hydroxycinnamoyl CoA shikimate hydroxycinnamoyl transferase, cinnamoyl CoA reductase, and cinnamyl alcohol dehydrogenase leads to lignin reduction in rice (Oryza sativa L. ssp. japonica cv. Nipponbare)
Plant Biotechnol. Rep.
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17-27
2017
Oryza sativa Japonica Group (Q6K9A2)
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brenda
Shi, C.; Qi, B.; Wang, X.; Shen, L.; Luo, J.; Zhang, Y.
Proteomic analysis of the key mechanism of exocarp russet pigmentation of semi-russet pear under rainwater condition
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2019
Pyrus pyrifolia (F4Y9E7)
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brenda
Smith, R.A.; Cass, C.L.; Mazaheri, M.; Sekhon, R.S.; Heckwolf, M.; Kaeppler, H.; de Leon, N.; Mansfield, S.D.; Kaeppler, S.M.; Sedbrook, J.C.; Karlen, S.D.; Ralph, J.
Suppression of cinnamoyl-CoA reductase increases the level of monolignol ferulates incorporated into maize lignins
Biotechnol. Biofuels
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109
2017
Zea mays
brenda
Park, H.L.; Bhoo, S.H.; Kwon, M.; Lee, S.W.; Cho, M.H.
Biochemical and expression analyses of the rice cinnamoyl-CoA reductase gene family
Front. Plant Sci.
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2099
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Oryza sativa Japonica Group
brenda
Yan, X.; Liu, J.; Kim, H.; Liu, B.; Huang, X.; Yang, Z.; Lin, Y.J.; Chen, H.; Yang, C.; Wang, J.P.; Muddiman, D.C.; Ralph, J.; Sederoff, R.R.; Li, Q.; Chiang, V.L.
CAD1 and CCR2 protein complex formation in monolignol biosynthesis in Populus trichocarpa
New Phytol.
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2019
Populus trichocarpa
brenda
Borah, P.; Khurana, J.P.
The OsFBK1 E3 ligase subunit affects anther and root secondary cell wall thickenings by mediating turnover of a cinnamoyl-CoA reductase
Plant Physiol.
176
2148-2165
2018
Oryza sativa
brenda
De Meester, B.; de Vries, L.; Oezparpucu, M.; Gierlinger, N.; Corneillie, S.; Pallidis, A.; Goeminne, G.; Morreel, K.; De Bruyne, M.; De Rycke, R.; Vanholme, R.; Boerjan, W.
Vessel-specific reintroduction of CINNAMOYL-COA REDUCTASE1 (CCR1) in dwarfed ccr1 mutants restores vessel and xylary fiber integrity and increases biomass
Plant Physiol.
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611-633
2018
Arabidopsis thaliana
brenda
Chao, N.; Li, S.; Li, N.; Qi, Q.; Jiang, W.T.; Jiang, X.N.; Gai, Y.
Two distinct cinnamoyl-CoA reductases in Selaginella moellendorffii offer insight into the divergence of CCRs in plants
Planta
246
33-43
2017
Selaginella moellendorffii, Selaginella moellendorffii (A0A1V0HSA2)
brenda
Wang, Z.; Ge, Q.; Wang, Z.
Concerning the role of cinnamoyl CoA reductase gene in phenolic acids biosynthesis in Salvia miltiorrhiza
Russ. J. Plant Physiol.
64
553-559
2017
Salvia miltiorrhiza
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brenda
Chao, N.; Jiang, W.T.; Wang, X.C.; Jiang, X.N.; Gai, Y.
Novel motif is capable of determining CCR and CCR-like proteins based on the divergence of CCRs in plants
Tree Physiol.
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2019-2026
2019
Vitis vinifera, Pinus koraiensis, Oryza sativa Indica Group, Pinus massoniana, Ziziphus jujuba
brenda