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Information on EC 1.2.1.44 - cinnamoyl-CoA reductase
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1.2.1.44 cinnamoyl-CoA reductaseIUBMB Comments
Acts also on a number of substituted cinnamoyl esters of coenzyme A.
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Word Map
- 1.2.1.44
- lignin
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cinnamyl
- monolignols
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phenylpropanoids
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lignification
- xylem
- caffeoyl-coa
- p-coumaroyl-coa
- leucocephala
- ccoaomt
- leucaena
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4-coumarate:coa
- gunnii
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sinapoyl
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guaiacyl
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syringyl
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cinnamyl-alcohol
- coniferaldehyde
- sinapoyl-coa
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lignin-specific
- sinapaldehyde
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non-condensed
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thioacidolysis
- biotechnology
- synthesis
- industry
- agriculture
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
cinnamoyl-coa reductase, cinnamoyl coa reductase, ll-ccrh1, bpccr1, cinnamoyl-coa reductase 1, ta-ccr2, sbccr1, atccr1, osccr1, sbccr2-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cinnamoyl-CoA:NADPH reductase
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cinnamoyl-coenzyme A reductase
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feruloyl coenzyme A reductase
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feruloyl-CoA reductase
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ferulyl-CoA reductase
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p-hydroxycinnamoyl coenzyme A reductase
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reductase, cinnamoyl coenzyme A
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cinnamaldehyde + CoA + NADP+ = cinnamoyl-CoA + NADPH + H+
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. In the first catalytic step, pro-R hydride transfer occurs from the C4 atom of NADPH to the reactive thioester carbonyl. The resulting oxyanion is temporarily stabilized by the oxyanion hole established from the side chain hydroxyl groups of Ser149 and Tyr183. Collapse of the tetrahedral intermediate is then followed by C-S bond cleavage and protonation of the CoA thiolate, in the presence of NADP+, there is very low affinity for the CoA ester compounds, which precludes the formation of a nonproductive complex, catalytic mechanism and substrate specificity, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -
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
59929-39-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
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-
?
additional information
?
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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
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
feruloyl-CoA + NADPH + H+
coniferaldehyde + CoA + NADP+
best substrate
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
thermodynamics and Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
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the highest expression levels of the three CCR genes occur in stem. The expression levels of SbCCR1 and SbCCR2-2 in stem and root are higher than in spikelet and leaf, but those of SbCCR2-1 in stem and spikelet are higher than in leaf and root. The gene copy number of SbCCR1 is significantly higher than those of SbCCR2-1 and SbCCR2-2 in root, leaf, stem and spikelet, especially in stem
additional information
the highest expression levels of the three CCR genes occur in stem. The expression levels of SbCCR1 and SbCCR2-2 in stem and root are higher than in spikelet and leaf, but those of SbCCR2-1 in stem and spikelet are higher than in leaf and root. The gene copy number of SbCCR1 is significantly higher than those of SbCCR2-1 and SbCCR2-2 in root, leaf, stem and spikelet, especially in stem
additional information
the highest expression levels of the three CCR genes occur in stem. The expression levels of SbCCR1 and SbCCR2-2 in stem and root are higher than in spikelet and leaf, but those of SbCCR2-1 in stem and spikelet are higher than in leaf and root. The gene copy number of SbCCR1 is significantly higher than those of SbCCR2-1 and SbCCR2-2 in root, leaf, stem and spikelet, especially in stem
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
T154Y mutation in SbCCR1 leads to broader substrate specificity and faster turnover
metabolism
physiological function
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
metabolism
cinnamoyl-CoA reductase (CCR) is the first enzyme in the monolignol-specific branch of the lignin biosynthetic pathway
metabolism
the enzyme is involved in the the monolignol biosynthetic pathway
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
the enzyme is involved in drought defense
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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the enzyme contains an NADP binding domain, an NWYCY domain, and a substrate domain
additional information
the enzyme contains an NADP binding domain, an NWYCY domain, and a substrate domain
additional information
the enzyme contains an NADP binding domain, an NWYCY domain, and a substrate domain
additional information
three-dimensional enzyme structure analysis and comparisons, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme in complex with NADP+, hanging drop, vapor diffusion method, mixing of 20 mg/ml protein in 20 mM Tris base, pH 7.5, 2 mM DTT, and 1 mM NADP+, with an equal volume of reservoir solution , containing 100 mM Bis-Tris, pH 6.5, and 25% w/v PEG 3350, and equilibration against reservoir solution at 4°C, X-ray diffraction structure determination and analysis at 2.35 A resolution, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme CCR1 from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography, anion exchange chromatography, and dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CCR1, recombinant His-tagged enzyme expression in Escherichia coli strain Rosetta (DE3)
gene SbCCR1, DNA and amino acid sequence determination and analysis, cloning and expression in Escherichia coli strain DH5alpha, phylogenetic analysis, recombinant expression of GFP-tagged enzyme in Nicotiana benthaminana leaves via Agrobacterum tumefaciens transfection, quantitative real-time PCR enzyme expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced by drought treatment, genes SbCCR1 and SbCCR2-2 mainly respond in the first phase of drought defense, while the SbCCR2-1 gene responds during the whole drought defense period
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
4
e2005
2016
Sorghum bicolor, Sorghum bicolor (C5XWV7), Sorghum bicolor (C5YLL4)
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