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Literature summary for 1.1.1.22 extracted from

  • Kandiba, L.; Eichler, J.
    AglM and VNG1048G, two haloarchaeal UDP-glucose dehydrogenases, show different salt-related behaviors (2016), Life, 6, pii: E31.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Inhibitors Comment Organism Structure
NaCl VNG1048G loses much of its activity when salinity drops below 3 M NaCl Halobacterium salinarum

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl AglM is active in 2-4 M NaCl Haloferax volcanii

Molecular Weight [Da]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Halobacterium salinarum Q9HQQ9
-
-
Halobacterium salinarum ATCC 700922 Q9HQQ9
-
-
Haloferax volcanii D4GYH5
-
-
Haloferax volcanii ATCC 29605 D4GYH5
-
-

Purification (Commentary)

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

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 [micromol/min/mg]

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 and Products (Substrate)

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

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

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
9.2
-
assay at Haloferax volcanii
9.2
-
assay at Halobacterium salinarum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Haloferax volcanii
NAD+
-
Halobacterium salinarum

General Information

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