Literature summary for 5.1.3.14 extracted from

Velloso, L.M.; Bhaskaran, S.S.; Schuch, R.; Fischetti, V.A.; Stebbins, C.E.
A structural basis for the allosteric regulation of non-hydrolysing UDP-GlcNAc 2-epimerases. [Erratum to document cited in CA148:302197] (2008), EMBO Rep., 9, 1251.

No PubMed abstract available

Activating Compound

Activating Compound	Comment	Organism	Structure
UDP-GlcNAc	allosteric activitation by substrate via direct interactions between UDP and substrate	Bacillus anthracis

Crystallization (Commentary)

Crystallization (Comment)	Organism
ternary complex between the UDP-GlcNAc 2-epimerase, its substrate UDP-GlcNAc and the reaction intermediate UDP, at 1.7 A resolution. Direct interactions between the substrate and UDP via two hydrogen bonds to the alpha- and beta-phosphates of the adjacent UDP molecule, and between the complex and highly conserved enzyme residues. The binding of UDP-GlcNAc is associated with conformational changes in the active site of the enzyme	Bacillus anthracis

Crystallization (Comment)

Organism

ternary complex between the UDP-GlcNAc 2-epimerase, its substrate UDP-GlcNAc and the reaction intermediate UDP, at 1.7 A resolution. Direct interactions between the substrate and UDP via two hydrogen bonds to the alpha- and beta-phosphates of the adjacent UDP molecule, and between the complex and highly conserved enzyme residues. The binding of UDP-GlcNAc is associated with conformational changes in the active site of the enzyme

Bacillus anthracis

Protein Variants

Protein Variants	Comment	Organism
H242A	dramatic decrease in catalytic efficiency	Bacillus anthracis
H44Q	dramatic decrease in catalytic efficiency	Bacillus anthracis
Q43A	dramatic decrease in catalytic efficiency	Bacillus anthracis
Q70A	dramatic decrease in catalytic efficiency	Bacillus anthracis
R210A	dramatic decrease in catalytic efficiency	Bacillus anthracis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
2.2	-	UDP-N-acetyl-D-glucosamine	wild-type	Bacillus anthracis
7.3	-	UDP-N-acetyl-D-glucosamine	mutant H44Q	Bacillus anthracis
10.4	-	UDP-N-acetyl-D-glucosamine	mutant H242A	Bacillus anthracis
11.1	-	UDP-N-acetyl-D-glucosamine	mutant Q70A	Bacillus anthracis
17.2	-	UDP-N-acetyl-D-glucosamine	mutant Q43A	Bacillus anthracis
20.9	-	UDP-N-acetyl-D-glucosamine	mutant R210A	Bacillus anthracis

Organism

Organism	UniProt	Comment	Textmining
Bacillus anthracis	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-N-acetyl-D-glucosamine	non-hydrolizing	Bacillus anthracis	UDP-N-acetyl-D-mannosamine	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.021	-	UDP-N-acetyl-D-glucosamine	mutant R210A	Bacillus anthracis
0.022	-	UDP-N-acetyl-D-glucosamine	mutant H242A	Bacillus anthracis
1.2	-	UDP-N-acetyl-D-glucosamine	mutant Q43A	Bacillus anthracis
2.06	-	UDP-N-acetyl-D-glucosamine	mutant Q70A	Bacillus anthracis
4	-	UDP-N-acetyl-D-glucosamine	mutant H44Q	Bacillus anthracis
7.9	-	UDP-N-acetyl-D-glucosamine	wild-type	Bacillus anthracis