Literature summary for 1.1.1.335 extracted from

Thoden, J.; Holden, H.
Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid (2010), Biochemistry, 49, 7939-7948.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pseudomonas aeruginosa
expression in Escherichia coli	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the enzyme in a complex with NAD(H), to 1.5 A resolution. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft	Pseudomonas aeruginosa
crystal structures of the enzyme in a complex with NAD(H) and 2-oxoglutarate, and the enzyme in a complex with NAD(H) and its substrate UDP-N-acetyl-D-glucosaminuronic acid, to 1.45 A and 2.0 A resolution, respectively. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft. Residues Lys101 and His185 most likely play key roles in catalysis	Thermus thermophilus

Crystallization (Comment)

Organism

crystal structure of the enzyme in a complex with NAD(H), to 1.5 A resolution. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft

Pseudomonas aeruginosa

crystal structures of the enzyme in a complex with NAD(H) and 2-oxoglutarate, and the enzyme in a complex with NAD(H) and its substrate UDP-N-acetyl-D-glucosaminuronic acid, to 1.45 A and 2.0 A resolution, respectively. The tetrameric enzyme assumes an unusual quaternary structure with the dinucleotides positioned quite closely to one another. Both 2-oxoglutarate and the UDP-linked sugar bind in the enzyme active site with their carbon atoms, C-2 and C-3', respectively, abutting the re face of the cofactor. They are positioned about 3 A from the nicotinamide C-4. The UDP-linked sugar substrate adopts a highly unusual curved conformation when bound in the enzyme's active site cleft. Residues Lys101 and His185 most likely play key roles in catalysis

Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	G3XD23	-	-
Thermus thermophilus	Q72KX8	-	-

Synonyms

Synonyms	Comment	Organism
WblA	-	Pseudomonas aeruginosa
WblA	-	Thermus thermophilus