EC Number   |
Reference |
|---|
   4.1.2.47 | - |
5149, 650346, 747927 |
| 4.1.2.47 | acetone-complexed crystals belong to the tetragonal space group P4(1)2(1)2 with unit-cell parameters a = 105.5 A, c = 188.5 A. Chloroacetone-complexed crystals are isomorphous to acetone-complexed crystals, with unit-cell parameters a = 105.9 A and c = 188.4 A |
649152 |
| 4.1.2.47 | crystal structure of the hydroxynitrile lyase at 1.9 A resolution. The structure belongs to the alpha/beta hydrolase superfamily. Its active site is deeply buried inside the protein, and connected to the outside by a narrow tunnel. The catalytic triade consists of residues Ser80, His235 and Asp207. By analogy with other alpha/beta hydrolases, the oxyanion hole is formed by the mainchain-NH of Cys81 and by the side-chains of Cys81 and Thr11 |
5150 |
| 4.1.2.47 | crystals obtained by sitting drop vapor diffusion, space group C222(1), unit cell dimensions a = 47.29 A, b = 106.66 A, c = 128.16 A |
650439 |
| 4.1.2.47 | enzyme in complex with acetone, hexafluoroacetone, trichloroacetaldehyde or rhodanine, hanging-drop vapour diffusion method, space group C222(1) |
653823 |
| 4.1.2.47 | hanging drop vapor diffusion method, freeze-quench method to prepare crystals of the complex of the enzyme with acetone cyanohydrin, complex of mutant K236L enzyme with acetone, structure of the K236L with acetone cyanohydrin-acetone cyanohydrin shows the substrate in a different orientation from the wild-type complex |
662210 |
| 4.1.2.47 | hanging drop vapor diffusion. crystal structures of hydroxynitrile lyase: one native and three complexes with acetone, isopropyl alcohol, and thiocyanate |
693103 |
| 4.1.2.47 | hanging-drop vapor-diffusion method. The crystals belong to the orthorhombic space group C222(1) with cell dimensions of a = 47.6, b = 106.8 and c = 128.2 A. The crystals diffract to about 2.5 A resolution on a rotating-anode X-ray source |
701457 |
| 4.1.2.47 | sitting drop vapor diffusion method, two crystal structures of Baliospermum montanum hydroxynitrile lyase, apo1 and apo2, are determined at 2.55 and 1.9 A, respectively. Structural comparison between Baliospermum montanum (apo2) and S-hydroxynitrile lyase from Hevea brasiliensis with (S)-mandelonitrile bound to the active site reveal that hydrophobic residues at the entrance region of Baliospermum montanum hydroxynitrile lyase form hydrophobic interactions with the benzene ring of the substrate. The flexible structures of these hydrophobic residues are confirmed by a 15 ns molecular dynamics simulation. This flexibility regulates the size of the active site cavity, enabling binding of various substrates to Baliospermum montanum. The high affinity of Baliospermum montanum hydroxynitrile lyase toward substrates containing a benzene ring is also confirmed by comparing the kinetics of Baliospermum montanum hydroxynitrile lyase and S-hydroxynitrile lyase from Manihot esculenta |
747168 |
| 4.1.2.47 | three-dimensional structure analysis, catalytic triad consisting of serine, histidine and aspartic acid |
671565 |
