Literature summary for 5.1.3.37 extracted from

Rozeboom, H.J.; Bjerkan, T.M.; Kalk, K.H.; Ertesvag, H.; Holtan, S.; Aachmann, F.L.; Valla, S.; Dijkstra, B.W.
Structural and mutational characterization of the catalytic A-module of the mannuronan C-5-epimerase AlgE4 from Azotobacter vinelandii (2008), J. Biol. Chem., 283, 23819-23828.

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.1 A resolution. Isoform AlgE4A folds into a right-handed parallel beta-helix structure. The alpha-helix is composed of four parallel beta-sheets, comprising 12 complete turns, and has an amphipathic alpha-helix near the N terminus. The catalytic site is positioned in a positively charged cleft formed by loops extending from the surface encompassing Asp152, an amino acid important for the reaction	Azotobacter vinelandii

Crystallization (Comment)

Organism

to 2.1 A resolution. Isoform AlgE4A folds into a right-handed parallel beta-helix structure. The alpha-helix is composed of four parallel beta-sheets, comprising 12 complete turns, and has an amphipathic alpha-helix near the N terminus. The catalytic site is positioned in a positively charged cleft formed by loops extending from the surface encompassing Asp152, an amino acid important for the reaction

Azotobacter vinelandii

Protein Variants

Protein Variants	Comment	Organism
D173E	54% residual activity	Azotobacter vinelandii
D178E	complete loss of activity	Azotobacter vinelandii
D178N	complete loss of activity	Azotobacter vinelandii
F122Y	65% residual activity	Azotobacter vinelandii
H154F	complete loss of activity	Azotobacter vinelandii
H154R	complete loss of activity	Azotobacter vinelandii
K117 R	24% residual activity	Azotobacter vinelandii
K117A	16% residual activity	Azotobacter vinelandii
K255A	8% residual activity	Azotobacter vinelandii
K255R	51% residual activity	Azotobacter vinelandii
P153A	10% residual activity	Azotobacter vinelandii
P153A/D173E	4% residual activity	Azotobacter vinelandii
Q156A	10% residual activity	Azotobacter vinelandii
Q225A	9% residual activity	Azotobacter vinelandii
Q225E	4% residual activity	Azotobacter vinelandii
Q225N	6% residual activity	Azotobacter vinelandii
R249A	46% residual activity	Azotobacter vinelandii
Y149F	complete loss of activity	Azotobacter vinelandii
Y149H	complete loss of activity	Azotobacter vinelandii

Organism

Organism	UniProt	Comment	Textmining
Azotobacter vinelandii	Q44493	-	-