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Literature summary for 1.1.1.24 extracted from

  • Carrington, Y.; Guo, J.; Le, C.H.; Fillo, A.; Kwon, J.; Tran, L.T.; Ehlting, J.
    Evolution of a secondary metabolic pathway from primary metabolism shikimate and quinate biosynthesis in plants (2018), Plant J., 95, 823-833 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene QDH2, phylogenetic analysis Populus trichocarpa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics Populus trichocarpa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-quinate + NAD+ Populus trichocarpa
-
3-dehydroquinate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Populus trichocarpa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-quinate + NAD+
-
Populus trichocarpa 3-dehydroquinate + NADH + H+
-
r

Synonyms

Synonyms Comment Organism
PoptrQDH2
-
Populus trichocarpa
QDH
-
Populus trichocarpa
QDH2
-
Populus trichocarpa

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Populus trichocarpa
NADH
-
Populus trichocarpa

General Information

General Information Comment Organism
evolution the enzyme belongs to the QDH family, phylogenetic reconstruction of the SDH/QDH gene family across land plants, overview. SDH and QDH belong to the same gene family, which diverged into two phylogenetic clades after a defining gene duplication just prior to the angiosperm/gymnosperm split. Non-seed plants that diverged before this duplication harbour only a single gene of this family. Extant representatives from the chlorophytes (Chlamydomonas reinhardtii), bryophytes (Physcomitrella patens) and lycophytes (Selaginella moellendorfii) encoded almost exclusively SDH activity in vitro. A reconstructed ancestral sequence representing the node just prior to the gene duplication also encoded SDH activity. Quinate dehydrogenase activity was gained only in seed plants following gene duplication. Quinate dehydrogenases of gymnosperms, e.g. Pinus taeda, may be reminiscent of an evolutionary intermediate since they encode equal SDH and QDH activities. The second copy in Pinus taeda maintains specificity for shikimate similar to the activity found in the angiosperm SDH sister clade. The codon for a tyrosine residue within the active site displays a signature of positive selection at the node defining the QDH clade, where it changed to a glycine. Replacing the tyrosine with a glycine in a highly shikimate-specific angiosperm SDH is sufficient to gain some QDH function. Thus, very few mutations are necessary to facilitate the evolution of QDH genes. The two proteins from Pinus taeda are chosen to represent the post-duplication SDH and QDH clades from gymnosperms. The single-copy genes from Selaginella moellendorffii, Physcomitrella patens and Chlamydomonas reinhardtii are selected to represent the pre-duplication lycopod, bryophyte and green algal clades, respectively. Thr381 is conserved in most members across all SDH clades but was replaced under positive selection by Gly in the branch leading into the seed plant QDH clade Populus trichocarpa
metabolism link between reactions catalysed by the shikimate pathway enzyme dehydroquinate dehydratase (DQD)/shikimate dehydrogenase (SDH) and quinate dehydrogenase (QDH) involved in quinate metabolism. Shikimate is produced from dehydroquinate via a two-step reaction and subsequently channelled to downstream reactions in the pathway. Quinate is reversibly formed from a side branch of the shikimate pathway from dehydroquinate and may be converted to more structurally complex secondary metabolites or to dehydroquinate to fuel the shikimate pathway Populus trichocarpa