Cloned (Comment) | Organism |
---|---|
gene UgdG, overexpression of His6-tagged enzyme in Escherichia coli | Sphingomonas elodea |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
47200 | - |
- |
Sphingomonas elodea |
48500 | - |
- |
Sphingomonas elodea |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Sphingomonas elodea | A4UTT2 | - |
- |
Sphingomonas elodea ATCC 31461 | A4UTT2 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography to over 95% purity | Sphingomonas elodea |
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 |
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 | 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 | Comment | Organism |
---|---|---|
UDP-glucose dehydrogenase | - |
Sphingomonas elodea |
UgdG | - |
Sphingomonas elodea |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Sphingomonas elodea |
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 |