Information on EC 1.2.1.44 - cinnamoyl-CoA reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.1.44
-
RECOMMENDED NAME
GeneOntology No.
cinnamoyl-CoA reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cinnamaldehyde + CoA + NADP+ = cinnamoyl-CoA + NADPH + H+
show the reaction diagram
also acts on a number of substituted cinnamoyl esters of coenzyme A
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
capsiconiate biosynthesis
-
-
Metabolic pathways
-
-
phenylpropanoid biosynthesis
-
-
Phenylpropanoid biosynthesis
-
-
phenylpropanoid biosynthesis
-
-
suberin monomers biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating)
Acts also on a number of substituted cinnamoyl esters of coenzyme A.
CAS REGISTRY NUMBER
COMMENTARY hide
59929-39-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
peanut
-
-
Manually annotated by BRENDA team
swede root
-
-
Manually annotated by BRENDA team
Eucalyptus sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
L. var. Mandarin, soybean
-
-
Manually annotated by BRENDA team
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Swissprot
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
cultivar Trichobel
UniProt
Manually annotated by BRENDA team
poplar
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
Swissprot
Manually annotated by BRENDA team
L. cv. La Victoire, infected with Agrobacterium rhizogenes
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
the enzyme carries out the first committed step in monolignol biosynthesis and acts as a first regulatory point in lignin formation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
show the reaction diagram
4-coumaroyl-CoA + NADPH + H+
4-coumaric aldehyde + CoA + NADP+
show the reaction diagram
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
show the reaction diagram
5-hydroxyferuloyl-CoA + NADPH
5-hydroxyferulic aldehyde + CoA + NADP+
show the reaction diagram
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
show the reaction diagram
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyferulic aldehyde + CoA + NADP+
show the reaction diagram
-
-
-
?
5-hydroxyferuloyl-CoA + NADPH + H+
? + CoA + NADP+
show the reaction diagram
-
-
-
r
caffeoyl-CoA + NADPH
caffeic aldehyde + CoA + NADP+
show the reaction diagram
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
show the reaction diagram
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
show the reaction diagram
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
show the reaction diagram
cinnamoyl-CoA + NADPH
cinnamaldehyde + CoA + NADP+
show the reaction diagram
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
show the reaction diagram
-
-
-
?
coniferaldehyde + CoA + NADP+
feruloyl-CoA + NADPH + H+
show the reaction diagram
-
-
-
-
r
coumaroyl-CoA + NADPH + H+
coumaraldehyde + CoA + NADP+
show the reaction diagram
activity assay
-
-
?
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
show the reaction diagram
feruloyl-CoA + NADPH
ferulic aldehyde + CoA + NADP+
show the reaction diagram
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
show the reaction diagram
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
show the reaction diagram
p-coumaroyl-CoA + NADPH
p-coumaric aldehyde + CoA + NADP+
show the reaction diagram
p-coumaroyl-CoA + NADPH + H+
p-coumaraldehyde + CoA + NADP+
show the reaction diagram
sinapaldehyde + CoA + NADP+
sinapoyl-CoA + NADPH + H+
show the reaction diagram
-
-
-
-
r
sinapoyl-CoA + NADPH
sinapic aldehyde + CoA + NADP+
show the reaction diagram
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-coumaroyl-CoA + NADPH + H+
4-coumaraldehyde + CoA + NADP+
show the reaction diagram
-
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaric aldehyde + CoA + NADP+
show the reaction diagram
Q08GL0
-
-
-
?
4-coumaroyl-CoA + NADPH + H+
4-coumaroylaldehyde + CoA + NADP+
show the reaction diagram
5-hydroxyferuloyl-CoA + NADPH + H+
5-hydroxyconiferaldehyde + CoA + NADP+
show the reaction diagram
5-hydroxyferuloyl-CoA + NADPH + H+
? + CoA + NADP+
show the reaction diagram
D2IX40, D2IX45
-
-
-
r
caffeoyl-CoA + NADPH + H+
caffealdehyde + CoA + NADP+
show the reaction diagram
caffeoyl-CoA + NADPH + H+
caffeolylaldehyde + CoA + NADP+
show the reaction diagram
cinnamaldehyde + CoA + NADP+
cinnamoyl-CoA + NADPH + H+
show the reaction diagram
cinnamoyl-CoA + NADPH + H+
cinnamaldehyde + CoA + NADP+
show the reaction diagram
D3J7Z3
-
-
-
?
coniferaldehyde + CoA + NADP+
feruloyl-CoA + NADPH + H+
show the reaction diagram
-
-
-
-
r
coumaroyl-CoA + NADPH + H+
coumaric aldehyde + CoA + NADP+
show the reaction diagram
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
show the reaction diagram
feruloyl-CoA + NADPH + H+
ferulic aldehyde + CoA + NADP+
show the reaction diagram
sinapaldehyde + CoA + NADP+
sinapoyl-CoA + NADPH + H+
show the reaction diagram
-
-
-
-
r
sinapoyl-CoA + NADPH + H+
sinapaldehyde + CoA + NADP+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
addition of Mg2+, Mn2+, Zn2+, Fe2+ has no effect
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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-
4-chloromercuribenzoate
5-Hydroxyferuloyl-CoA
Ca2+
-
86% residual activity at 2 mM
caffeoyl-CoA
competitive inhibitor
citraconic anhydride
-
31% residual activity at 1.5 mM with feruloyl-CoA as substrate
Co2+
-
42% residual activity at 2 mM
CoASH
-
product inhibition
Cs2+
-
83% residual activity at 2 mM
Cu2+
-
49% residual activity at 2 mM
Diethylpyrocarbonate
-
44% residual activity at 3 mM with feruloyl-CoA as substrate
Fe2+
-
92% residual activity at 2 mM
Feruloyl-CoA
Hg2+
-
complete inhibition at 2 mM
iodoacetamide
-
1 mM, 50% inhibition
Mg2+
-
74% residual activity at 2 mM
Mn2+
-
21% residual activity at 2 mM
N-acetyl imidazole
-
50% residual activity at 3 mM with feruloyl-CoA as substrate
N-ethylmaleimide
-
-
NADP+
-
product inhibition
Ni2+
-
25% residual activity at 2 mM
Phenylglyoxal
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47% residual activity at 1 mM with feruloyl-CoA as substrate
phenylmethylsulfonyl fluoride
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60% residual activity at 1 mM with feruloyl-CoA as substrate
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(3,4-dimethoxyphenyl)ethenyl]phosphonothioate
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S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3,5-dimethoxyphenyl)ethenyl]phosphonothioate
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-
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]phosphonothioate
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S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxyphenyl)ethenyl]phosphonothioate
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S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-methoxyphenyl)ethenyl]phosphonothioate
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-
SDS
-
6% residual activity at 1% (v/v)
Sinapoyl-CoA
competitive inhibitor
Woodward's reagent K
-
54% residual activity at 0.02 mM with feruloyl-CoA as substrate
Zn2+
-
45% residual activity at 2 mM
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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-
bovine serum albumin
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twofold increase of enzyme activity
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dithiothreitol
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-
OsRac1
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interaction with OsRac1, one of the Rac/Rop family of small GTPases, lead to the enzymatic activation of OsCCR1 in vitro
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sphingolipid elicitor
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induction of expression
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Triton X-100
-
106% activity at 1% (v/v)
Tween 20
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113% activity at 1% (v/v)
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028 - 0.0572
4-Coumaroyl-CoA
0.0346 - 0.1824
5-Hydroxyferuloyl-CoA
0.00516 - 0.2
caffeoyl-CoA
0.9
cinnamoyl-CoA
-
-
0.031 - 0.05
coniferaldehyde
0.06
coumaroyl-CoA
-
in 100 mM phosphate buffer pH 6.5, at 30C
0.00042 - 0.244
Feruloyl-CoA
0.0116 - 0.29
NADPH
0.00227 - 0.1
p-Coumaroyl-CoA
0.039 - 0.067
sinapaldehyde
0.00055 - 0.4
Sinapoyl-CoA
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.188 - 0.32
4-Coumaroyl-CoA
4.9
5-Hydroxyferuloyl-CoA
Populus tremuloides
Q9M631
-
0.0145 - 113
caffeoyl-CoA
94 - 236
coniferaldehyde
0.43 - 105
coumaroyl-CoA
0.0372 - 164
Feruloyl-CoA
1.63
p-Coumaroyl-CoA
Arabidopsis thaliana
-
-
81 - 210
sinapaldehyde
0.013 - 131
Sinapoyl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2400
caffeoyl-CoA
Leucaena leucocephala
-
in 100 mM phosphate buffer pH 6.5, at 30C
537
1900 - 7500
coniferaldehyde
3680
1700
coumaroyl-CoA
Leucaena leucocephala
-
in 100 mM phosphate buffer pH 6.5, at 30C
5236
310 - 4600
Feruloyl-CoA
427
1200 - 5300
sinapaldehyde
5214
2300
Sinapoyl-CoA
Leucaena leucocephala
-
in 100 mM phosphate buffer pH 6.5, at 30C
1333
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0157
5-Hydroxyferuloyl-CoA
competitive inhibition of 5-hydroxyferuloyl-CoA on the feruloyl-CoA reaction
0.0153
caffeoyl-CoA
competitive inhibition of caffeoyl-CoA on the feruloyl-CoA reaction
0.0063 - 0.0083
Feruloyl-CoA
0.031 - 0.156
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(3,4-dimethoxyphenyl)ethenyl]phosphonothioate
0.0071 - 0.055
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3,5-dimethoxyphenyl)ethenyl]phosphonothioate
0.0044 - 0.057
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]phosphonothioate
0.212 - 0.422
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-hydroxyphenyl)ethenyl]phosphonothioate
0.068 - 0.29
S-[2-(acetylamino)ethyl] O-ethyl [(E)-2-(4-methoxyphenyl)ethenyl]phosphonothioate
0.02
Sinapoyl-CoA
competitive inhibition of sinapoyl-CoA on the feruloyl-CoA reaction
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
feruloyl-CoA as a substrate at pH 7.0
0.02
feruloyl-CoA as a substrate at pH 6.5
0.1
feruloyl-CoA as a substrate at pH 5.0
0.12
feruloyl-CoA as a substrate at pH 5.5
0.14
feruloyl-CoA as a substrate at pH 6.0
1.78
-
with feruloyl-CoA as substrate
16.2
-
-
17.15
-
-
84.07
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3 - 6.5
-
-
6 - 6.2
-
-
6
activity assay, feruloyl-CoA as substrate
6.2
activity assay; activity assay
7.4 - 7.8
-
-
7.5
-
forward reaction
7.8
-
reverse reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 6.5
when the pH is above 6.5, the activity becomes negligible, feruloyl-CoA as substrate
5.4 - 8
-
pH 5.4: about 10% of activity maximum, pH 8.0: about 15% of activity maximum
additional information
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-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
below and above 25C, gradual loss in the enzyme activity is recorded
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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cambium sap, mainly from cambial and young xylem cells
Manually annotated by BRENDA team
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active lignifying tissue
Manually annotated by BRENDA team
Alamo cultivar; Alamo cultivar
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
gel filtration
35700
x * 35700, calculated from amino acid sequence
36600
-
AtCCR2, predicted from gene sequence
36800
predicted molecular mass for CCR1 and CCR2; predicted molecular mass for CCR1 and CCR2
37000
-
determined by SDS-PAGE
37400
x * 37400, deduced from gene sequence
38700
-
1 * 38700, SDS-PAGE
39420
calculated molecular mass
40000
-
gel filtration
43000
x * 43000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
-
the enzyme is most stable around pH 6.5 at 25C for 90 min, while at pH 6.0 and 7.0, the enzyme is stable for 45 and 60 min, respectively
725147
7
-
30C, 30 min, most stable around
288230
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
-
the enzyme is stable for 60 min at 25C and at optimum temperature 30C, stability is observed for 40 min. However, at 20C and 35C, 36% and 42% loss in activity is observed after 60 min. Above 40C, significant loss in Ll-CCRH1 activity is observed within 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol: stabilizes , only stable in presence of
ethyleneglycol, 15%, stabilizes
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 100 mM Tris-HCl buffer, pH 7.5, 10% ethyleneglycol, several weeks
-
-20C, presence of: NADP+, 2-mercaptoethanol, ethyleneglycol, several months
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4C, mercaptoethanol, ethyleneglycol, 1 month, 35% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
as His-tagged enzyme by means of Ni-NTA beads; as His-tagged enzyme by means of Ni-NTA beads
by gel filtration, to homogeneity
CCR protein is purified using a Bug-Buster GSTclosed circleBind purification kit, and the fused tag is cleaved and removed using the Enterokinase Cleavage capture kit
partial, two forms
-
recombinant fusion proteins GST-AtCCR1 and GST-AtCCR2, expressed in Escherichia coli
-
recombinant proteins are purified on a glutathione resin; recombinant proteins are purified on a glutathione resin
using a glutathione-sepharose 4 Fast Flow column, purified GST-AtCCR1 is cleaved by thrombin to remove the GST tag
-
using Ni-NTA His-Bind resin
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned into the pET-29b vector and expressed in Escherichia coli strains BL21(DE3), BL21(DE3)pLysS, RIL, and RP
expressed in Escherichia coli BL21 (DE34) cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Nicotiana tabacum variety Xanthi via Agrobacterium tumefaciens strain LBA4404
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five-year-old transgenic plants of Norway spruce Picea abies expressing the Norway spruce gene encoding CCR in antisense orientation under the control of the maize ubiquitin promoter
for generation of RNAi constructs and for tomato transformation through Agrobacterium tumefaciens, into the pGEX4T-1 vector for expression in Escherichia coli BL21 cells; for generation of RNAi constructs and for tomato transformation through Agrobacterium tumefaciens, into the pGEX4T-1 vector for expression in Escherichia coli BL21 cells
for the construction of a yeast two-hybrid assay prey vectors containing different fragments of OsCCR1 are made by using the pVP16 vector, for transient expression in rice protoplasts a OsCCR1-GFP construct is generated, full length OsCCR1 is cloned into a pET30 vector for expression in Escherichia coli cells
-
heterologous expression as His-tagged fusion protein in Escherichia coli; heterologous expression as His-tagged fusion protein in Escherichia coli
into the pET41a+ and pET23b+ vector for expression in Escherichia coli BL21DE3 cells
into the pGEX-4T vector for expression in Escherichia coli BL21DE3 cells
-
introduction of four different constructs into poplar (Populus tremula x Populus alba)
-
production of active enzyme in Escherichia coli
-
specific PCR product is cloned into the pGEM-T Easy vector, as an expression vector for Escherichia coli, pET28a is used
two genes AtCCR1 and AtCCR2, localised on chromosome 1, AtCCR1 is associated with lignin biosynthesis during development, AtCCR2 is associated with the hypersensitive response to pathogen attack; two recombinant proteins expressed in Escherichia coli
-
two genes ZmCCR1 and ZmCCR2, ZmCCR1 is involved in constitutive lignification, function of ZmCCR2 unknown
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression can be induced by exposure to Xanthomonas campestris pv. Campestris or methyl jasmonate. Enzyme expression is highest in old roots, flowers, and young leaves
knockout of caffeoyl CoA 3-O-methyltransferase up-regulates isoform CCR2
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
I31N
-
the mutant demonstrates better affinity for sinapoyl CoA over others
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
S212G
-
the mutant exhibits the catalytic efficiencies less than 10% of wild type enzyme; the mutant shows a 2.5fold increase in Km, 7fold reduction in kcat and 15fold decrease in kcat/Km
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
V200E
-
the mutant shows reduced catalytic efficiency compared to the wild type
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry
additional information