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Aldehyde dehydrogenase
From Proteopedia
(Difference between revisions)
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*ALDH class 2 | *ALDH class 2 | ||
| - | **[[3n80]], [[1o05]] – hALDH2 residues 18-517- human<BR /> | + | **[[3n80]], [[1o05]], [[4kwf]] – hALDH2 residues 18-517- human<BR /> |
**[[3n81]], [[2onn]], [[2ono]], [[1zum]] – hALDH2 residues 18-517 (mutant) <BR /> | **[[3n81]], [[2onn]], [[2ono]], [[1zum]] – hALDH2 residues 18-517 (mutant) <BR /> | ||
**[[1ag8]] – bALDH NAD binding domain - bovine | **[[1ag8]] – bALDH NAD binding domain - bovine | ||
| Line 51: | Line 51: | ||
*ALDH2 binary complex | *ALDH2 binary complex | ||
| - | **[[3inj]], [[3inl]] - hALDH2 residues 18-517 + agonist<BR /> | + | **[[3inj]], [[3inl]], [[4kwg]] - hALDH2 residues 18-517 + agonist<BR /> |
**[[2vle]] - hALDH2 residues 24-517 + daidzin<BR /> | **[[2vle]] - hALDH2 residues 24-517 + daidzin<BR /> | ||
**[[1nzx]], [[1nzz]], [[1o00]], [[1o02]], [[1cw3]] - hALDH2 residues 18-517 + NAD<BR /> | **[[1nzx]], [[1nzz]], [[1o00]], [[1o02]], [[1cw3]] - hALDH2 residues 18-517 + NAD<BR /> | ||
| Line 68: | Line 68: | ||
**[[1ad3]] – rALDH3<br /> | **[[1ad3]] – rALDH3<br /> | ||
**[[3sza]] - hALDH3A1<br /> | **[[3sza]] - hALDH3A1<br /> | ||
| - | **[[3szb]] – hALDH3A1 + inhibitor<br /> | + | **[[3szb]], [[4l1o]], [[4l2o]] – hALDH3A1 + inhibitor<br /> |
**[[4h80]] - hALDH3A1 (mutant) + inhibitor<br /> | **[[4h80]] - hALDH3A1 (mutant) + inhibitor<br /> | ||
**[[4qgk]] – hALDH3A2 + ligand<br /> | **[[4qgk]] – hALDH3A2 + ligand<br /> | ||
| Line 77: | Line 77: | ||
**[[2w8p]] - Succinate–semi-hALDH family 5 (mutant) <BR /> | **[[2w8p]] - Succinate–semi-hALDH family 5 (mutant) <BR /> | ||
**[[3r31]] – Betaine-ALDH – ''Agrobacterium tumefaciens''<BR /> | **[[3r31]] – Betaine-ALDH – ''Agrobacterium tumefaciens''<BR /> | ||
| - | **[[3ed6]], [[4mpb]], [[4nu9]] - Betaine-SaALDH – ''Staphylococcus aureus''<BR /> | + | **[[3ed6]], [[4mpb]], [[4nu9]], [[4q92]], [[4qto]] - Betaine-SaALDH – ''Staphylococcus aureus''<BR /> |
| + | **[[4qje]] - Betaine-SaALDH (mutant)<br /> | ||
| + | **[[4cbb]] - Betaine-PaALDH - ''Pseudomonas aeruginosa''<br /> | ||
**[[1a4s]] - Betaine-cALDH - cod<BR /> | **[[1a4s]] - Betaine-cALDH - cod<BR /> | ||
**[[3llg]], [[3tz6]], [[3vos]] – Aspartate-semi-MtALDH<BR /> | **[[3llg]], [[3tz6]], [[3vos]] – Aspartate-semi-MtALDH<BR /> | ||
| Line 93: | Line 95: | ||
**[[2w8q]] - Succinate–semi-hALDH family 5 + succinic acid<BR /> | **[[2w8q]] - Succinate–semi-hALDH family 5 + succinic acid<BR /> | ||
**[[3fg0]], [[4mpy]], [[4nea]] - Betaine-SaALDH + NAD<BR /> | **[[3fg0]], [[4mpy]], [[4nea]] - Betaine-SaALDH + NAD<BR /> | ||
| - | **[[4ni4]] - Betaine-SaALDH (mutant) + NAD<br /> | + | **[[4ni4]], [[4qn2]] - Betaine-SaALDH (mutant) + NAD<br /> |
**[[1bpw]] - Betaine-cALDH + NAD<BR /> | **[[1bpw]] - Betaine-cALDH + NAD<BR /> | ||
**[[2j6l]] – Aminoadipate-semi-hALDH family 7 + NAD<BR /> | **[[2j6l]] – Aminoadipate-semi-hALDH family 7 + NAD<BR /> | ||
**[[2cfi]] - Formyltetrahydrofolate-hALDH hydrolase domain + formyltetrahydropterin<BR /> | **[[2cfi]] - Formyltetrahydrofolate-hALDH hydrolase domain + formyltetrahydropterin<BR /> | ||
| - | **[[2nad]] - Formate- | + | **[[2nad]] - Formate-PaALDH + NAD <BR /> |
**[[1bi9]] – Retinal-rALDH2 + NAD<BR /> | **[[1bi9]] – Retinal-rALDH2 + NAD<BR /> | ||
**[[3l4p]], [[1sij]] – ALDH + AsO3 – ''Desulfovibrio gigas''<br /> | **[[3l4p]], [[1sij]] – ALDH + AsO3 – ''Desulfovibrio gigas''<br /> | ||
**[[4a0m]] – spALDH + NAD – spinach<br /> | **[[4a0m]] – spALDH + NAD – spinach<br /> | ||
**[[3iwk]] – amino-ALDH + NAD – pea<br /> | **[[3iwk]] – amino-ALDH + NAD – pea<br /> | ||
| - | **[[3ju8]] - Succinylglutamic–semi-PaALDH + NAD | + | **[[3ju8]] - Succinylglutamic–semi-PaALDH + NAD <br /> |
| + | **[[4caz]] - Betaine-PaALDH + NAD derivative<br /> | ||
**[[4c3s]] - ALDH + NAD – ''Clostridium phytofermentans''<br /> | **[[4c3s]] - ALDH + NAD – ''Clostridium phytofermentans''<br /> | ||
**[[4i3u]] – SmALDH + phosphonoacetaldehyde<br /> | **[[4i3u]] – SmALDH + phosphonoacetaldehyde<br /> | ||
| Line 123: | Line 126: | ||
**[[3rh9]] - Succinate–semi-ALDH – ''Marinobacter aquaeolei''<br /> | **[[3rh9]] - Succinate–semi-ALDH – ''Marinobacter aquaeolei''<br /> | ||
**[[3uw3]] - aspartate–semi-ALDH – ''Burkholderia thailandensis''<br /> | **[[3uw3]] - aspartate–semi-ALDH – ''Burkholderia thailandensis''<br /> | ||
| - | **[[3v4c]] - SmALDH | + | **[[3v4c]] - SmALDH<br /> |
| + | **[[4gac]] – ALDH – mouse<br /> | ||
*NADP-dependent ALDH binary complexes | *NADP-dependent ALDH binary complexes | ||
| Line 136: | Line 140: | ||
**[[3jz4]] - Succinate–semi-EcALDH + NADP<br /> | **[[3jz4]] - Succinate–semi-EcALDH + NADP<br /> | ||
**[[3hsk]] - aspartate–semi-ALDH + NADP – ''Candida albicans''<br /> | **[[3hsk]] - aspartate–semi-ALDH + NADP – ''Candida albicans''<br /> | ||
| - | **[[4h73]] - ALDH + NADP – ''Pyrobaculum''<br /> | + | **[[4h73]], [[4nmj]], [[4nmk]] - ALDH + NADP – ''Pyrobaculum''<br /> |
*NADP-dependent ALDH ternary complexes | *NADP-dependent ALDH ternary complexes | ||
| Line 144: | Line 148: | ||
**[[2vro]] – BxALDH + NADP + alcohol | **[[2vro]] – BxALDH + NADP + alcohol | ||
| + | *Uncharacterized ALDH | ||
| - | **[[3k9d]] – ALDH – ''Listeria monocytogenes'' | + | **[[3k9d]] – ALDH – ''Listeria monocytogenes''<br /> |
| + | **[[4dng]] – ALDH – ''Bacillus subtilis''<br /> | ||
| + | **[[3my7]] – ALDH – ''Vibrio parahaemolyticus''<br /> | ||
*Antiquitin | *Antiquitin | ||
| Line 151: | Line 158: | ||
**[[2jg7]] – Antiquitin – ''Acanthopagrus schlegeli'' | **[[2jg7]] – Antiquitin – ''Acanthopagrus schlegeli'' | ||
| - | **[[3my7]] – ALDH – ''Vibrio parahaemolyticus'' | ||
}} | }} | ||
==References== | ==References== | ||
Revision as of 12:13, 27 January 2015
Image:1nzx.png
Crystal Structure of Aldehyde dehydrogenase, 1nzx
Aldehyde dehydrogenase (ALDH) converts aldehydes to carboxylic acids while reducing NAD+ to NADH. In mammals there are 3 classes of ALDH and each contain constitutive and inducible forms.
- ALDH class 1 is cytosolic.
- ALDH class 2 is mitochondrial.
- ALDH class 3 is found in tumors, stomach and cornea. ALDH3A1 is soluble and has substrate specificity to bulky aromatic aldehydes. ALDH3A2 is a fatty ALDH (FALDH). FALDH was found to have an additional gatekeeper helix at the substrate funnel entrance that is shaping the enzymes substrate specificity. [1]
- ALDH family 7 member A1 is known as antiquitin and functions in the detoxification of aldehydes.
3D Structures of Aldehyde dehydrogenase
Updated on 27-January-2015
References
- ↑ Keller, Markus A.; Zander, Ulrich; Fuchs, Julian E.; Kreutz, Christoph; Watschinger, Katrin et al. (2014). A gatekeeper helix determines the substrate specificity of Sjögren–Larsson Syndrome enzyme fatty aldehyde dehydrogenase. Nature Communications vol. 5.
