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Literature summary for 1.2.1.44 extracted from

  • 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 (2014), Plant Cell, 26, 3709-3727 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.44

Application

Application Comment Organism
biotechnology potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants Medicago truncatula
biotechnology potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants Petunia x hybrida
synthesis potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants Medicago truncatula
synthesis potential exploitation of rationally engineered forms of CCR and CAD2 for the targeted modification of monolignol composition in transgenic plants Petunia x hybrida

Cloned(Commentary)

Cloned (Comment) Organism
gene CCR1, recombinant expression of His6-tagged enzyme in Escherichia coli Petunia x hybrida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2086
-
 4-coumaroyl-CoA recombinant isozyme CCR1, pH 6.0, 25°C Petunia x hybrida
0.2703
-
 sinapoyl-CoA recombinant isozyme CCR1, pH 6.0, 25°C Petunia x hybrida
0.3076
-
 feruloyl-CoA recombinant isozyme CCR1, pH 6.0, 25°C Petunia x hybrida

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-coumaroyl-CoA + NADPH + H+ Medicago truncatula
-
 4-coumaraldehyde + CoA + NADP+
-
 r
4-coumaroyl-CoA + NADPH + H+ Petunia x hybrida
-
 4-coumaraldehyde + CoA + NADP+
-
 r
caffeoyl-CoA + NADPH + H+ Medicago truncatula
-
 caffealdehyde + CoA + NADP+
-
 r
cinnamoyl-CoA + NADPH + H+ Medicago truncatula
-
 cinnamaldehyde + CoA + NADP+
-
 r
feruloyl-CoA + NADPH + H+ Medicago truncatula
-
 coniferaldehyde + CoA + NADP+
-
 r
feruloyl-CoA + NADPH + H+ Petunia x hybrida
-
 coniferaldehyde + CoA + NADP+
-
 r
sinapoyl-CoA + NADPH + H+ Medicago truncatula
-
 sinapaldehyde + CoA + NADP+
-
 r
sinapoyl-CoA + NADPH + H+ Petunia x hybrida
-
 sinapaldehyde + CoA + NADP+
-
 r

Organism

Organism UniProt Comment Textmining
Medicago truncatula
-
-
-
Medicago truncatula G7JEE5
-
-
Petunia x hybrida A0A059TC02
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration Petunia x hybrida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-coumaroyl-CoA + NADPH + H+
-
 Medicago truncatula 4-coumaraldehyde + CoA + NADP+
-
 r
4-coumaroyl-CoA + NADPH + H+
-
 Petunia x hybrida 4-coumaraldehyde + CoA + NADP+
-
 r
caffeoyl-CoA + NADPH + H+
-
 Medicago truncatula caffealdehyde + CoA + NADP+
-
 r
caffeoyl-CoA + NADPH + H+ low activity Medicago truncatula caffealdehyde + CoA + NADP+
-
 r
cinnamoyl-CoA + NADPH + H+
-
 Medicago truncatula cinnamaldehyde + CoA + NADP+
-
 r
feruloyl-CoA + NADPH + H+
-
 Medicago truncatula coniferaldehyde + CoA + NADP+
-
 r
feruloyl-CoA + NADPH + H+
-
 Petunia x hybrida coniferaldehyde + CoA + NADP+
-
 r
feruloyl-CoA + NADPH + H+ best substrate Petunia x hybrida coniferaldehyde + CoA + NADP+
-
 r
feruloyl-CoA + NADPH + H+ preferred substrate for isozyme CCR1 Medicago truncatula coniferaldehyde + CoA + NADP+
-
 r
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 Medicago truncatula ?
-
 ?
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 Medicago truncatula ?
-
 ?
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 Petunia x hybrida ?
-
 ?
sinapoyl-CoA + NADPH + H+
-
 Medicago truncatula sinapaldehyde + CoA + NADP+
-
 r
sinapoyl-CoA + NADPH + H+
-
 Petunia x hybrida sinapaldehyde + CoA + NADP+
-
 r

Synonyms

Synonyms Comment Organism
CCR
-
 Medicago truncatula
CCR
-
 Petunia x hybrida
CCR1
-
 Medicago truncatula
CCR1
-
 Petunia x hybrida
CCR2
-
 Medicago truncatula
cinnamoyl-CoA reductase1
-
 Medicago truncatula
cinnamoyl-CoA reductase1
-
 Petunia x hybrida
cinnamoyl-CoA reductase2
-
 Medicago truncatula
Ph-CCR1
-
 Petunia x hybrida

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Petunia x hybrida

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 CCR1 melting temperature is 33°C in absence of ligands and 43-45 in presence of ligands, effect of added ligands, NADP+ and CoA, on melting temperature of Petunia hybrida CCR1 isozyme, overview Petunia x hybrida
additional information
-
 CCR1 melting temperature is 35°C in absence of ligands and 42-47 in presence of ligands, effect of added ligands, NADP+ and CoA, on melting temperature of Medicago truncatula CCR2 isozyme, overview Medicago truncatula

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.2
-
 4-coumaroyl-CoA recombinant isozyme CCR1, pH 6.0, 25°C Petunia x hybrida
3.4
-
 sinapoyl-CoA recombinant isozyme CCR1, pH 6.0, 25°C Petunia x hybrida
5.8
-
 feruloyl-CoA recombinant isozyme CCR1, pH 6.0, 25°C Petunia x hybrida

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Petunia x hybrida

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Medicago truncatula
NADP+ binding structure analysis. Structural comparisons of the NADP+-complexed form of Ph-CCR1 with the apo forms of both Ph-CCR1 and Medicago trunculata Mt-CCR2 reveals a number of adjustments that are localized to polypeptide chain segments surrounding the central cleft and are undoubtedly a direct consequence of NADP+ binding Medicago truncatula
NADP+ binding structure analysis. Structural comparisons of the NADP+-complexed form of Ph-CCR1 with the apo forms of both Ph-CCR1 and Medicago trunculata Mt-CCR2 reveals a number of adjustments that are localized to polypeptide chain segments surrounding the central cleft and are undoubtedly a direct consequence of NADP+ binding Petunia x hybrida
NADPH
-
 Medicago truncatula
NADPH
-
 Petunia x hybrida

General Information

General Information Comment Organism
metabolism cinnamoyl-CoA reductase and cinnamyl-alcohol dehydrogenase are key enzymes of monolignol biosynthesis Petunia x hybrida
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 Medicago truncatula
additional information structural comparisons of various liganded and unliganded forms of cinnamoyl-CoA reductase, CCR, and CAD2, cinnamyl alcohol dehydrogenase, overview Medicago truncatula
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 Petunia x hybrida

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6
-
 4-coumaroyl-CoA recombinant isozyme CCR1, pH 6.0, 25°C Petunia x hybrida
12.6
-
 sinapoyl-CoA recombinant isozyme CCR1, pH 6.0, 25°C Petunia x hybrida
18.7
-
 feruloyl-CoA recombinant isozyme CCR1, pH 6.0, 25°C Petunia x hybrida