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Literature summary for 1.1.1.22 extracted from

  • Yurist-Doutsch, S.; Magidovich, H.; Ventura, V.V.; Hitchen, P.G.; Dell, A.; Eichler, J.
    N-glycosylation in Archaea: on the coordinated actions of Haloferax volcanii AglF and AglM (2010), Mol. Microbiol., 75, 1047-1058.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
NaCl is able to function in a variety of salt concentrations, enzymatic activity improves as salinity decreases. At 4 M NaCl concentration the enzyme was able to produce 870 nM NADH, while at 0.5 M NaCl, over 1.5 mM NADH is produced 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 the enzyme is involved in protein N-glycosylation UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O Haloferax volcanii DSM 3757 the enzyme is involved in protein N-glycosylation UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
?

Organism

Organism UniProt Comment Textmining
Haloferax volcanii D4GYH5
-
-
Haloferax volcanii DSM 3757 D4GYH5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-alpha-D-glucose + 2 NAD+ + H2O the enzyme is involved in protein N-glycosylation Haloferax volcanii UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme Haloferax volcanii UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O the enzyme is involved in protein N-glycosylation Haloferax volcanii DSM 3757 UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
?
UDP-alpha-D-glucose + 2 NAD+ + H2O while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme Haloferax volcanii DSM 3757 UDP-alpha-D-glucuronate + 2 NADH + 2 H+
-
?
UDP-alpha-D-mannose + 2 NAD+ + H2O while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme Haloferax volcanii UDP-alpha-D-mannuronate + 2 NADH + 2 H+
-
?
UDP-alpha-D-mannose + 2 NAD+ + H2O while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme Haloferax volcanii DSM 3757 UDP-alpha-D-mannuronate + 2 NADH + 2 H+
-
?
UDP-D-galactose + 2 NAD+ + H2O while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme Haloferax volcanii UDP-alpha-D-galacturonate + 2 NADH + 2 H+
-
?
UDP-D-galactose + 2 NAD+ + H2O while the enzyme is able to process various sugar nucleotides, of those compounds tested, UDP-glucose is by far the preferred substrate of the enzyme Haloferax volcanii DSM 3757 UDP-alpha-D-galacturonate + 2 NADH + 2 H+
-
?

Synonyms

Synonyms Comment Organism
AglM
-
Haloferax volcanii
HVO_1531 locus name Haloferax volcanii
UDP-glucose dehydrogenase
-
Haloferax volcanii

General Information

General Information Comment Organism
malfunction Haloferax volcanii cells deleted of HVO_1531 present a modified S-layer Haloferax volcanii
physiological function the enzyme is involved in protein N-glycosylation Haloferax volcanii