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Literature summary for 1.1.1.195 extracted from

  • Trabucco, G.M.; Matos, D.A.; Lee, S.J.; Saathoff, A.J.; Priest, H.D.; Mockler, T.C.; Sarath, G.; Hazen, S.P.
    Functional characterization of cinnamyl alcohol dehydrogenase and caffeic acid O-methyltransferase in Brachypodium distachyon (2013), BMC Biotechnol., 13, 61.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene CAD5 or Bradi3g06480, sequence comparisons of the CAD family enzymes from different species, phylogenetic tree Brachypodium distachyon

Protein Variants

Protein Variants Comment Organism
additional information BdCAD1 targeted silencing via highly specific artificial microRNA, Transgenic growth and developmental phenotype, overview. Downregulation of BdCAD1 is associated with a significant decrease in S units and a slight yet not statistically significant increase in G units, resulting in a reduced S/G ratio in lignin composition Brachypodium distachyon

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall
-
Brachypodium distachyon 5618
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required, the enzyme contains the Zn-1 binding domain motif GHE(X)2G(X)5G(X)2V and the conserved Zn-1 catalytic residues C47, H69, and C163 Brachypodium distachyon

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cinnamyl alcohol + NADP+ Brachypodium distachyon
-
cinnamaldehyde + NADPH + H+
-
r

Organism

Organism UniProt Comment Textmining
Brachypodium distachyon I1HY48
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf low enzyme level Brachypodium distachyon
-
root
-
Brachypodium distachyon
-
stem highly expressed in developing stem. Of the seven CAD genes identified in Brachypodium distachyon, BdCAD1 expression is greatest in stem tissue, exhibiting 10fold higher transcript level than any of the other seven BdCAD genes Brachypodium distachyon
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cinnamyl alcohol + NADP+
-
Brachypodium distachyon cinnamaldehyde + NADPH + H+
-
r

Synonyms

Synonyms Comment Organism
BdCAD1
-
Brachypodium distachyon
Bradi3g06480
-
Brachypodium distachyon
CAD
-
Brachypodium distachyon
CAD5
-
Brachypodium distachyon
cinnamyl alcohol dehydrogenase
-
Brachypodium distachyon

Cofactor

Cofactor Comment Organism Structure
additional information the enzyme has a highly conserved Rossmann fold NAD(P)H/NAD(P)+ binding domain Brachypodium distachyon
NADP+
-
Brachypodium distachyon
NADPH
-
Brachypodium distachyon

General Information

General Information Comment Organism
evolution CAD tends to exist in multi-gene families with one gene being primarily responsible for lignin biosynthesis. The BdCAD family consists of Bradi3g06480 (BdCAD1), Bradi3g17920 (BdCAD2), Bradi3g22980 (BdCAD3), Bradi4g29770 (BdCAD4), Bradi4g29780 (BdCAD5), Bradi5g04130 (BdCAD6), and Bradi5g21550 (BdCAD7) Brachypodium distachyon
malfunction transgenic silencing of BdCAD1 causes altered flowering time and increases stem count and weight. Downregulation of BdCAD1 causes a leaf brown midrib phenotype. While acetyl bromide soluble lignin measurements are equivalent in BdCAD1 downregulated and control plants, histochemical staining and thioacidolysis indicate a decrease in lignin syringyl units and reduced syringyl/guaiacyl ratio in the transgenic plants. The perturbed enzyme results in greater stem biomass yield and bioconversion efficiency Brachypodium distachyon
metabolism cinnamyl alcohol dehydrogenase and caffeic acid O-methyltransferase catalyze key steps in the pathway of lignin monomer biosynthesis Brachypodium distachyon
additional information only BdCAD1 contains both active substrate binding residues, W119 and F298, which determine specificity for aromatic alcohols, and the conserved S212 residue that determines NADP(H) binding at that position Brachypodium distachyon
physiological function cinnamyl-alcohol dehydrogenase functions in one of the final steps of monolignol biosynthesis that catalyzes the reduction of cinnamyl aldehyde to cinnamyl alcohol prior to polymerization into the lignin polymer. It appears that BdCAD1 (Bradi3g06480) contains the conserved functional and structural features of a medium chain dehydrogenase/reductase specific to enzymes involved in lignin biosynthesis in secondary cell walls Brachypodium distachyon