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Literature summary for 1.1.1.22 extracted from

  • Barbas, A.; Popescu, A.; Frazao, C.; Arraiano, C.; Fialho, A.
    Rossmann-fold motifs can confer multiple functions to metabolic enzymes: RNA binding and ribonuclease activity of a UDP-glucose dehydrogenase (2013), Biochem. Biophys. Res. Commun., 430, 218-224.
    View publication on PubMed
Search for more literature for 1.1.1.22

Cloned(Commentary)

Cloned (Comment) Organism
gene UgdG, overexpression of His6-tagged enzyme in Escherichia coli Sphingomonas elodea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47200
-
-
 Sphingomonas elodea
48500
-
-
 Sphingomonas elodea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-alpha-D-glucose + 2 NAD+ + H2O Sphingomonas elodea
-
 UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
 ?
UDP-alpha-D-glucose + 2 NAD+ + H2O Sphingomonas elodea ATCC 31461
-
 UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
 ?

Organism

Organism UniProt Comment Textmining
Sphingomonas elodea A4UTT2
-
-
Sphingomonas elodea ATCC 31461 A4UTT2
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography to over 95% purity Sphingomonas elodea

Reaction

Reaction Comment Organism Reaction ID
UDP-alpha-D-glucose + 2 NAD+ + H2O = UDP-alpha-D-glucuronate + 2 NADH + 2 H+ the enzyme is also binds RNA and acts as a ribonuclease Sphingomonas elodea
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is also not only able to bind RNA but also acts as a ribonuclease. The ribonucleolytic activity occurs independently of the presence of NAD+ and the RNA binding site does not coincide with the NAD+ binding region, kinetics of interaction between UgdG and RNA, overview. The Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease Sphingomonas elodea ?
-
 ?
additional information the enzyme is also not only able to bind RNA but also acts as a ribonuclease. The ribonucleolytic activity occurs independently of the presence of NAD+ and the RNA binding site does not coincide with the NAD+ binding region, kinetics of interaction between UgdG and RNA, overview. The Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease Sphingomonas elodea ATCC 31461 ?
-
 ?
UDP-alpha-D-glucose + 2 NAD+ + H2O
-
 Sphingomonas elodea UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
 ?
UDP-alpha-D-glucose + 2 NAD+ + H2O
-
 Sphingomonas elodea ATCC 31461 UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
 ?

Subunits

Subunits Comment Organism
? x * 48500, recombinant His6-tagged enzyme, SDS-PaGE, x * 47200, native enzyme, SDS-PAGE Sphingomonas elodea
More the Rossmann structural motifs found in NAD+-dependent dehydrogenases can have a dual function working as a nucleotide cofactor binding domain and as a ribonuclease Sphingomonas elodea

Synonyms

Synonyms Comment Organism
UDP-glucose dehydrogenase
-
 Sphingomonas elodea
UgdG
-
 Sphingomonas elodea

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Sphingomonas elodea

General Information

General Information Comment Organism
evolution the N- and C-terminal domains of UgdG share structural features with ancient mitochondrial ribonucleases named MAR. MARs are present in lower eukaryotic microorganisms, have a Rossmannoid-fold and belong to the isochorismatase superfamily Sphingomonas elodea
physiological function the enzyme provides UDP-glucuronic acid for the synthesis of the exopolysaccharide gellan Sphingomonas elodea