Aldehyde dehydrogenase

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Line 45: Line 45:
*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-PsALDH + NAD – ''Pseudomonas''<BR />
+
**[[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 – ''Pseudomonas aeruginosa''<br />
+
**[[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

Template:STRUCTURE 1o9j











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

  1. 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.

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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