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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.195 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

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.195 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)

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.195 Brachypodium distachyon I1HY48
-
-
2.1.1.68 Brachypodium distachyon I1I1F5
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.195 leaf low enzyme level Brachypodium distachyon
-
1.1.1.195 root
-
 Brachypodium distachyon
-
1.1.1.195 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
-
2.1.1.68 stem high expression in developing stem Brachypodium distachyon
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.1.1.195 BdCAD1
-
 Brachypodium distachyon
1.1.1.195 Bradi3g06480
-
 Brachypodium distachyon
1.1.1.195 CAD
-
 Brachypodium distachyon
1.1.1.195 CAD5
-
 Brachypodium distachyon
1.1.1.195 cinnamyl alcohol dehydrogenase
-
 Brachypodium distachyon
2.1.1.68 Bradi3g16530
-
 Brachypodium distachyon
2.1.1.68 COMT4
-
 Brachypodium distachyon

Cofactor

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

General Information

EC Number General Information Comment Organism
1.1.1.195 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
1.1.1.195 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
1.1.1.195 metabolism cinnamyl alcohol dehydrogenase and caffeic acid O-methyltransferase catalyze key steps in the pathway of lignin monomer biosynthesis Brachypodium distachyon
1.1.1.195 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
1.1.1.195 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
2.1.1.68 physiological function transgenic plants overexpressing artificial microRNA to silence BdCOMT4 show altered flowering time and increased stem count and weight. Downregulated plants exhibit a reduction in total lignin content and decreased Maule staining of syringyl units in stem Brachypodium distachyon