Journal:Acta Cryst F:S2053230X23004430
From Proteopedia
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Aldehyde dehydrogenase (ALDH) plays an important role in aldehyde detoxification. Acetaldehyde is also considered carcinogenic and toxic. Thermostable ALDH from the hyperthermophilic archaeon ''Sulfolobus tokodaii'' (ALDHSt), exhibits high activity toward acetaldehyde and has potential applications as a biosensor for acetaldehyde. This structural information provides clues regarding the mechanisms of substrate recognition and thermostability in ALDH. | Aldehyde dehydrogenase (ALDH) plays an important role in aldehyde detoxification. Acetaldehyde is also considered carcinogenic and toxic. Thermostable ALDH from the hyperthermophilic archaeon ''Sulfolobus tokodaii'' (ALDHSt), exhibits high activity toward acetaldehyde and has potential applications as a biosensor for acetaldehyde. This structural information provides clues regarding the mechanisms of substrate recognition and thermostability in ALDH. | ||
| - | <scene name='96/967852/Homotetramer/3'>The ALDHSt homotetramer</scene> is a dimer of dimers (A/B and C/D) with crystallographic 222 symmetry. | + | <scene name='96/967852/Homotetramer/3'>The ALDHSt homotetramer</scene> is a dimer of dimers (A/B and C/D) with crystallographic 222 symmetry. <scene name='96/967852/Monomer/1'>Structure of the monomer subunit</scene>. The cofactor-binding domain, catalytic domain and oligomerization domain are shown in green, cyan and magenta, respectively. NADP is shown as a yellow stick model. |
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<b>References</b><br> | <b>References</b><br> | ||
<references/> | <references/> | ||
</StructureSection> | </StructureSection> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
Revision as of 12:40, 29 May 2023
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
