Cloned (Comment) | Organism |
---|---|
gene aglM, recombinant expression of CBD-tagged and C-terminally poly-His-tagged enzyme | Haloferax volcanii |
gene udg1, recombinant expression of CBD-tagged and C-terminally poly-His-tagged enzyme | Halobacterium salinarum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
NaCl | VNG1048G loses much of its activity when salinity drops below 3 M NaCl | Halobacterium salinarum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
NaCl | AglM is active in 2-4 M NaCl | Haloferax volcanii |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
47000 | - |
- |
Haloferax volcanii |
47000 | - |
- |
Halobacterium salinarum |
99000 | - |
dimeric enzyme, gel filtration at 2 M NaCl | Halobacterium salinarum |
550000 | - |
dodecameric enzyme, gel filtration at 2 M NaCl | Halobacterium salinarum |
550000 | - |
gel filtration at 2 M NaCl | Haloferax volcanii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + 2 NAD+ + H2O | Haloferax volcanii | - |
UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? | |
UDP-alpha-D-glucose + 2 NAD+ + H2O | Halobacterium salinarum | - |
UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? | |
UDP-alpha-D-glucose + 2 NAD+ + H2O | Haloferax volcanii ATCC 29605 | - |
UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? | |
UDP-alpha-D-glucose + 2 NAD+ + H2O | Halobacterium salinarum ATCC 700922 | - |
UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Halobacterium salinarum | Q9HQQ9 | - |
- |
Halobacterium salinarum ATCC 700922 | Q9HQQ9 | - |
- |
Haloferax volcanii | D4GYH5 | - |
- |
Haloferax volcanii ATCC 29605 | D4GYH5 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant CBD- and poly-His-tagged enzyme by ultracentrifugation and nickel affinity chromatography | Haloferax volcanii |
recombinant CBD- and poly-His-tagged enzyme by ultracentrifugation and nickel affinity chromatography | Halobacterium salinarum |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | the organism grows optimally in 1.7-2.5 M NaCl | Haloferax volcanii | - |
additional information | the organism grows optimally in 3-5 M NaCl, requiring the higher salinity for proper growth and cell shape | Halobacterium salinarum | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.00000143 | - |
purified dodecameric enzyme, pH 9.2, temperature not specified in the publication | Halobacterium salinarum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
UDP-alpha-D-glucose + 2 NAD+ + H2O | - |
Haloferax volcanii | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? | |
UDP-alpha-D-glucose + 2 NAD+ + H2O | - |
Halobacterium salinarum | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? | |
UDP-alpha-D-glucose + 2 NAD+ + H2O | - |
Haloferax volcanii ATCC 29605 | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? | |
UDP-alpha-D-glucose + 2 NAD+ + H2O | - |
Halobacterium salinarum ATCC 700922 | UDP-alpha-D-glucuronate + 2 NADH + 2 H+ | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | 2 * 47000, about, SDS-PAGE | Halobacterium salinarum |
dodecamer | 12 * 47000, about, SDS-PAGE | Haloferax volcanii |
dodecamer | 12 * 47000, about, SDS-PAGE | Halobacterium salinarum |
More | sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview | Haloferax volcanii |
More | the specific activity of the VNG1048G dodecamer at 2 M NaCl is only one sixth of that of UDP-glucose dehydrogenase AglM, while the dimer is inactive. The oligomeric status of VNG1048G is affected by lowered salinity. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview | Halobacterium salinarum |
Synonyms | Comment | Organism |
---|---|---|
AglM | - |
Haloferax volcanii |
HVO_1531 | - |
Haloferax volcanii |
UDG1 | - |
Halobacterium salinarum |
UDP-glucose dehydrogenase | - |
Haloferax volcanii |
UDP-glucose dehydrogenase | - |
Halobacterium salinarum |
VNG1048G | - |
Halobacterium salinarum |
VNG_1048G | - |
Halobacterium salinarum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
9.2 | - |
assay at | Haloferax volcanii |
9.2 | - |
assay at | Halobacterium salinarum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Haloferax volcanii | |
NAD+ | - |
Halobacterium salinarum |
General Information | Comment | Organism |
---|---|---|
metabolism | in the Haloferax volcanii archaeal glycosylation pathway, Agl, responsible for the assembly and attachment of an Asn-linked pentasaccharide, enzyme AglM acts as a UDP-glucose dehydrogenase, converting UDP-glucose into UDP-glucuronic acid | Haloferax volcanii |
additional information | Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview | Haloferax volcanii |
additional information | surface-exposed residues in homology models of the UDP-glucose dehydrogenase reveals the more acidic and less basic VNG1048G surface, explaining the salt-dependence of the Halobacterium salinarum enzyme. Sequence and structure comparison of UDP-glucose dehydrogenase AglM from Haloferax volcanii and VNG1048G from Halobacterium salinarum, homology modelling, overview | Halobacterium salinarum |
physiological function | enzyme AglM can be functionally replaced by another UDP-glucose dehydrogenase, VNG1048G, in vivo | Haloferax volcanii |
physiological function | enzyme VNG1048G can functionally replace another UDP-glucose dehydrogenase AglM in vivo. In Halobacterium salinarum, where glycoproteins are modified by an N-linked glycan of similar composition, gene VNG1048G is not only found within a cluster of N-glycosylation-related genes reminiscent of the genomic region surrounding its Haloferax volcanii counterpart AglM but can also functionally replace gene aglM in a Haloferax volcanii strain lacking the gene | Halobacterium salinarum |