Sandbox Reserved 496: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 15: | Line 15: | ||
==='''Structure'''=== | ==='''Structure'''=== | ||
---- | ---- | ||
The CODH/ACS enzyme from M. thermoacetica is an α2β2 tetramer. Each β subunit (residues 2 to 674) carries out CODH activity, while each α subunit(residues 2 to 729) is responsible for ACS activity. | The CODH/ACS enzyme from M. thermoacetica is an α2β2 tetramer. Each β subunit (residues 2 to 674) carries out CODH activity, while each α subunit(residues 2 to 729) is responsible for ACS activity. The β subunit has 57% helical and 9% β-sheet character with 31 helices and 15 β-strands. Overall, the α subunit has 50% helical and 14% β-sheet character with 36 helices and 22 β-strands. | ||
==='''Mechanism of Action'''=== | ==='''Mechanism of Action'''=== | ||