Crystallization (Comment) | Organism |
---|---|
X-ray crystallography screening of ligands bound nucleophile mutant E115S, to 1 A resolution. Laminariheptaose binds in an arch with the reducing and nonreducing ends occupying either side of the catalytic cleft of the enzyme. alpha-Laminariheptaosyl fluoride can make a nucleophilic attack upon itself, the major product being a cyclic beta-1,3-heptaglucan. The cyclic laminariheptaose molecule is not completely planar and torsion angles at the glycosidic linkages fluctuate between two energy minima | Phanerodontia chrysosporium |
Protein Variants | Comment | Organism |
---|---|---|
E115S | X-ray crystallography screening of ligands bound nucleophile mutant E115S. Laminariheptaose binds in an arch with the reducing and nonreducing ends occupying either side of the catalytic cleft of the enzyme. R-laminariheptaosyl fluoride can make a nucleophilic attack upon itself, the major product being a cyclic beta-1,3-heptaglucan | Phanerodontia chrysosporium |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Phanerodontia chrysosporium | Q874E3 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-laminariheptaosyl fluoride | - |
Phanerodontia chrysosporium | ? | substrate can make a nucleophilic attack upon itself, the major product being a cyclic beta-1,3-heptaglucan. NMR confirms uniquely beta-1,3-linkages and no reducing end. The cyclic laminariheptaose molecule is not completely planar and torsion angles at the glycosidic linkages fluctuate between two energy minima | ? | |
laminariheptaose + H2O | - |
Phanerodontia chrysosporium | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
laminarinase 16A | - |
Phanerodontia chrysosporium |