Aldehyde dehydrogenase
From Proteopedia
(Difference between revisions)
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* '''ALDH class 2''' is mitochondrial. <br /> | * '''ALDH class 2''' is mitochondrial. <br /> | ||
* '''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. <ref>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.</ref><br /> | * '''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. <ref>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.</ref><br /> | ||
| - | * '''ALDH family 7 member A1''' is known as '''antiquitin''' and functions in the detoxification of aldehydes. | + | * '''ALDH family 7 member A1''' is known as '''antiquitin''' and functions in the detoxification of aldehydes. <br /> |
| + | * '''Glyceraldehyde-3-phophate (G3P)-ALDH''' is called GAPDH. GADPH catalyzes the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate (G3P) to 1,3-bisphosphoglycerate in the presence of inorganic phosphate (Pi) and NAD. A cysteine-thiol at the active site of GAPDH plays a role I catalysis. The aldehyde of G3P reacts with the cysteine-thiol to form a carboxylic acid in a high energy thioester form. The thioester is attacked by the inorganic phosphate and forms the acyl phosphate. GAPDH is part of the glycolysis pathway. GAPDH contains NAD-dependent and NADPH-dependent enzymes. | ||
== 3D Structures of Aldehyde dehydrogenase == | == 3D Structures of Aldehyde dehydrogenase == | ||
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**[[3lns]] - Benzaldehyde-PpALDH3 + NADP + benzoate<BR /> | **[[3lns]] - Benzaldehyde-PpALDH3 + NADP + benzoate<BR /> | ||
**[[2imp]] - Lactaldehyde-EcALDH + NADH + lactate<BR /> | **[[2imp]] - Lactaldehyde-EcALDH + NADH + lactate<BR /> | ||
| - | **[[2vro]] – BxALDH + NADP + alcohol | + | **[[2vro]] – BxALDH + NADP + alcohol <br /> |
| + | |||
| + | *NAD-dependent glyceraldehydes-3-phosphate dehydrogenase | ||
| + | |||
| + | **[[1vsu]] – CpGAPDH – ''Cryptosporidium parvum''<br /> | ||
| + | **[[1ywg]] – PfGAPDH – ''Plasmodium falciparum''<br /> | ||
| + | **[[3cmc]] - GAPDH – ''Bacillus stearothermophilus''<br /> | ||
| + | **[[2ep7]] – GAPDH – ''Aquifex aeolicus''<br /> | ||
| + | **[[2i5p]] – GAPDH – ''Kluyveromyces marxianus''<br /> | ||
| + | **[[1obf]] – GAPDH – ''Achromobacter xylosoxidans''<br /> | ||
| + | **[[1b7g]] – GAPDH – ''Sulfolobus solfataricus''<br /> | ||
| + | **[[2gd1]] – GsGAPDH – ''Geobacillus stearothermophilus''<br /> | ||
| + | **[[3e6a]] – OsGAPDH – ''Oryza sativa''<br /> | ||
| + | **[[4gpd]], [[1gpd]], [[1crw]] – GAPDH – lobster<br /> | ||
| + | **[[3l6o]], [[3lc7]] – SaGAPDH<br /> | ||
| + | **[[1dc3]], [[1dc5]], [[1s7c]] – EcGAPDH - ''Escherichia coli''<br /> | ||
| + | |||
| + | *''GAPDH binary complex'' | ||
| + | |||
| + | **[[1k3t]] - TcGAPDH + inhibitor<br /> | ||
| + | **[[3hja]] - GAPDH + NAD – ''Borellia burgdorferi''<br /> | ||
| + | **[[1vsv]], [[3cps]] - CpGAPDH + NAD<br /> | ||
| + | **[[2vyn]], [[2vyv]] - rGAPDH residues 102-432 + EcGAPDH + NAD<br /> | ||
| + | **[[2b4r]], [[2b4t]] – PfGAPDH (mutant) + NAD<br /> | ||
| + | **[[1j0x]] – GAPDH + NAD – rabbit<br /> | ||
| + | **[[1ihx]] – PvGAPDH + NAD <br /> | ||
| + | **[[1dss]], [[1szj]] - PvGAPDH NAD-binding and catalytic domains+ NAD<br /> | ||
| + | **[[1ihy]] – PvGAPDH + ADP-ribose<br /> | ||
| + | **[[1gyq]], [[1gyp]] - LmGAPDH + NAD derivative – ''Leishmania mexicana''<br /> | ||
| + | **[[1i32]], [[1i33]] – LmGAPDH + inhibitor<br /> | ||
| + | **[[1a7k]] – LmGAPDH + NAD<br /> | ||
| + | **[[1cer]], [[2g82]] - GAPDH + NAD – ''Thermus aquaticus''<br /> | ||
| + | **[[1gd1]] - GsGAPDH + NAD<br /> | ||
| + | **[[1npt]], [[1nq5]], [[1dbv]], [[2dbv]], [[3dbv]], [[4dbv]] - GsGAPDH (mutant) + NAD<br /> | ||
| + | **[[3e5r]] – OsGAPDH + NAD <br /> | ||
| + | **[[3k73]], [[3lvf]] – SaGAPDH + NAD<br /> | ||
| + | **[[3lc2]] - SaGAPDH + G3P<br /> | ||
| + | **[[3k9q]], [[3ksd]], [[3lc1]], [[3hq4]] - SaGAPDH (mutant) + NAD<br /> | ||
| + | **[[3gpd]], [[2u8f]], [[1znq]] – hGAPDH + NAD<br /> | ||
| + | **[[1gad]], [[1dc6]] - EcGAPDH + NAD<br /> | ||
| + | **[[1gae]] - EcGAPDH (mutant) + NAD<br /> | ||
| + | **[[1dc4]] – EcGAPDH + G3P<br /> | ||
| + | |||
| + | *''GAPDH ternary complex'' | ||
| + | |||
| + | **[[3id5]], [[3dmt]], [[1ml3]] – TcGAPDH + NAD + inhibitor <br /> | ||
| + | **[[1qxs]] - TcGAPDH + NAD + G3P analog<br /> | ||
| + | **[[3cif]] - CpGAPDH + NAD + G3P<br /> | ||
| + | **[[1nqa]], [[1nqo]] - GsGAPDH (mutant) + NAD + G3P<br /> | ||
| + | **[[3ksz]], [[3kv3]], [[3l4s]] - SaGAPDH (mutant) + NAD + G3P<br /> | ||
| + | |||
| + | *NADP-dependent GAPDH with cofactor NADP | ||
| + | |||
| + | **[[2dbv]], [[4dbv]] - GsGAPDH (mutant) + NADP<br /> | ||
| + | **[[2yyy]] - MjGAPDH + NADP<br /> | ||
| + | **[[2euh]] - SmGAPDH + NADP<br /> | ||
| + | **[[2id2]] - SmGAPDH (mutant) + NADP<br /> | ||
| + | **[[1cf2]] - GAPDH + NADP – ''Methanothermus fervidus''<br /> | ||
| + | **[[1jn0]], [[1rm4]], [[2pkq]], [[2pkr]] - sGAPDH + NADP<br /> | ||
| + | **[[1rm3]], [[1rm5]] - sGAPDH (mutant) + NADP<br /> | ||
| + | **[[1ky8]] - TtGAPDH + NADP – ''Thermoproteus tenax''<br /> | ||
| + | **[[3rhh]] - BhGAPDH + NADP<br /> | ||
| + | |||
| + | *''NADP-dependent GAPDH ternary complexes containing glyceraldehyde-3-phosphate (G3P)" | ||
| + | |||
| + | **[[1qi1]] - SmGAPDH + NADP + G3P<br /> | ||
| + | **[[2esd]], [[2qe0]] - SmGAPDH (mutant) + NADP + G3P<br /> | ||
| + | **[[3lc2]] – SaGAPDH-thioacyl + G3P<br /> | ||
| + | **[[1uxu]] - TtGAPDH (mutant) + NADP + AMP + G3P<br /> | ||
| + | |||
| + | *''Other NADP-dependent GAPDH ternary complexes'' | ||
| + | |||
| + | **[[1k3t]] - TcGAPDH + coumarin derivative <br /> | ||
| + | **[[1uxv]] - TtGAPDH + NADP + AMP<br /> | ||
| + | **[[1uxp]] - TtGAPDH (mutant) + NADP + ADP<br /> | ||
| + | **[[1uxq]] - TtGAPDH (mutant) + NADP + G1P<br /> | ||
| + | **[[1uxr]] - TtGAPDH (mutant) + NADP + F6P | ||
*Uncharacterized ALDH | *Uncharacterized ALDH | ||
Revision as of 06:47, 12 April 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.
- Glyceraldehyde-3-phophate (G3P)-ALDH is called GAPDH. GADPH catalyzes the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate (G3P) to 1,3-bisphosphoglycerate in the presence of inorganic phosphate (Pi) and NAD. A cysteine-thiol at the active site of GAPDH plays a role I catalysis. The aldehyde of G3P reacts with the cysteine-thiol to form a carboxylic acid in a high energy thioester form. The thioester is attacked by the inorganic phosphate and forms the acyl phosphate. GAPDH is part of the glycolysis pathway. GAPDH contains NAD-dependent and NADPH-dependent enzymes.
3D Structures of Aldehyde dehydrogenase
Updated on 12-April-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.
