Sandbox Reserved 313: Difference between revisions
No edit summary |
No edit summary |
||
| Line 26: | Line 26: | ||
[[Image: | [[Image:Proteopedia_113.jpg]] | ||
=Mechanism= | =Mechanism= | ||
It has been proposed that the mechanism of Bc-SMase is similar to that of bovine pancreatic DNase 1 because Bc-SMase and bovine DNase 1 are homologous proteins which both have conserved alleged catalytic amino acid residues and a similar molecular structure<ref name="gp">PMID: 16595670 </ref>. . The proposed hydrolytic activity of Bc-SMAse cloned from ''Bacillus cereus'' is coordinated by essential water bridged divalent metal ions. Two metal ions which are bound to the Glu-53 and <scene name='Sandbox_Reserved_313/His-296/2'>His-296</scene> residues in the central cleft which orientate the substrate in the active site. | It has been proposed that the mechanism of Bc-SMase is similar to that of bovine pancreatic DNase 1 because Bc-SMase and bovine DNase 1 are homologous proteins which both have conserved alleged catalytic amino acid residues and a similar molecular structure<ref name="gp">PMID: 16595670 </ref>. . The proposed hydrolytic activity of Bc-SMAse cloned from ''Bacillus cereus'' is coordinated by essential water bridged divalent metal ions. Two metal ions which are bound to the Glu-53 and <scene name='Sandbox_Reserved_313/His-296/2'>His-296</scene> residues in the central cleft which orientate the substrate in the active site. | ||