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Literature summary for 3.13.1.1 extracted from

  • Essigmann, B.; Hespenheide, B.M.; Kuhn, L.A.; Benning, C.
    Prediction of the active-site structure and NAD+ binding in SQD1, a protein essential for sulfolipid biosynthesis in Arabidopsis (1999), Arch. Biochem. Biophys., 369, 30-41.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
Arabidopsis thaliana 9507
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-glucose + ? Arabidopsis thaliana first step of sulfolipid biosynthesis, unknown sulfur donor UDP-sulfoquinovose + H2O
-
?
UDP-glucose + sulfite Arabidopsis thaliana
-
UDP-sulfoquinovose + H2O
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni2+-nitrilotriacetic acid column Arabidopsis thaliana

Reaction

Reaction Comment Organism Reaction ID
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite sequence similarity to sugar nucleotide modifying enzymes, Thr228 seems to be catalytically important Arabidopsis thaliana
UDP-alpha-D-sulfoquinovopyranose + H2O = UDP-alpha-D-glucose + sulfite short-chain dehydrogenase/reductase family Arabidopsis thaliana

Storage Stability

Storage Stability Organism
4°C, 50 mM MES buffer, pH 6.5, 10 mM UDP-glucose, stable for 10 days Arabidopsis thaliana
4°C, 50 mM MES buffer, pH 6.5, stable for 2-3 days Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-glucose + ? first step of sulfolipid biosynthesis, unknown sulfur donor Arabidopsis thaliana UDP-sulfoquinovose + H2O
-
?
UDP-glucose + sulfite
-
Arabidopsis thaliana UDP-sulfoquinovose + H2O
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+ tightly bound, enzyme binds 1 NAD+ per monomer, side-chain chemistry and hydrogen-bonding patterns in the NAD+ site Arabidopsis thaliana