Aldehyde dehydrogenase

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[[3my7]] – ALDH – ''Vibrio parahaemolyticus''
[[3my7]] – ALDH – ''Vibrio parahaemolyticus''
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==References==
==References==

Revision as of 07:30, 24 September 2014

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.

Contents

3D Structures of Aldehyde dehydrogenase

Updated on 24-September-2014

ALDH class 1

3fx4 – ALDH1 + NADP + inhibitor – pig
1bxs – ALDH1 - sheep
1o9j – ALDH1 + NAD – Elephant shrew
3rhj, 3rhl, 3rho, 3rhp, 3rhq, 3rhr – rALDH1 C- terminal (mutant) + NADP – rat
3rhm - rALDH1 C- terminal
1hso – hALDH1 α subunit + Zn + NAD
1ht0 – hALDH1 γ subunit (mutant) + Zn + NAD

ALDH class 2

3n80, 1o05 – hALDH2 residues 18-517- human
3n81, 2onn, 2ono, 1zum – hALDH2 residues 18-517 (mutant)
1ag8 – bALDH NAD binding domain - bovine

Binary complex

3inj, 3inl - hALDH2 residues 18-517 + agonist
2vle - hALDH2 residues 24-517 + daidzin
1nzx, 1nzz, 1o00, 1o02, 1cw3 - hALDH2 residues 18-517 + NAD
3n82, 3n83, 2onm, 2onp, 1nzw, 1o04 – hALDH2 residues 18-517 (mutant) + NADH
3sz9 - hALDH2 residues 18-517 + inhibitor
1a4z – bALDH2 NAD-binding domain + NAD

Ternary complex

1o01 - hALDH2 residues 18-517 + NADH + aldehyde
4fqf - hALDH2 residues 18-517 + NAD + NO2
4fr8 - hALDH2 residues 18-517 (mutant) + NAD + ADP + nitroglycerin

ALDH class 3

1ad3 – rALDH3
3sza - hALDH3A1
3szb – hALDH3A1 + inhibitor
4h80 - hALDH3A1 (mutant) + inhibitor
4qgk – hALDH3A2 + ligand

NAD-dependent ALDH

2w8n, 2w8o, 2w8r – Succinate–semi-hALDH family 5
2w8p - Succinate–semi-hALDH family 5 (mutant)
3r31 – Betaine-ALDH – Agrobacterium tumefaciens
3ed6, 4mpb, 4nu9 - Betaine-SaALDH – Staphylococcus aureus
1a4s - Betaine-cALDH - cod
3llg, 3tz6, 3vos – Aspartate-semi-MtALDH
2cq8 - Formyltetrahydrofolate-hALDH PP-binding domain - NMR
2nac – Formate-PsALDH
3i44 – ALDH – Bartonella henselae
3ek1 – ALDH – Brucella melitensis
3ros – ALDH – Lactobacillus acidophilus
3r64 – ALDH – Corynebacterium glutamicum
3rhe – Benzaldehyde-ALDH – Legionella pneumophila
3u4j, 4i3t – SmALDH – Sinorhizobium meliloti

Binary complexes

2w8q - Succinate–semi-hALDH family 5 + succinic acid
3fg0, 4mpy, 4nea - Betaine-SaALDH + NAD
4ni4 - Betaine-SaALDH (mutant) + NAD
1bpw - Betaine-cALDH + NAD
2j6l – Aminoadipate-semi-hALDH family 7 + NAD
2cfi - Formyltetrahydrofolate-hALDH hydrolase domain + formyltetrahydropterin
2nad - Formate-PsALDH + NAD – Pseudomonas
1bi9 – Retinal-rALDH2 + NAD
3l4p, 1sij – ALDH + AsO3 – Desulfovibrio gigas
4a0m – spALDH + NAD – spinach
3iwk – amino-ALDH + NAD – pea
3ju8 - Succinylglutamic–semi-PaALDH + NAD – Pseudomonas aeruginosa
4c3s - ALDH + NAD – Clostridium phytofermentans
4i3u – SmALDH + phosphonoacetaldehyde

Ternary complexes

2gsd – Formate-ALDH + NAD + azide – Moraxella
1nvm – Acetaldehyde-PsALDH + 4-hydroxy-oxovalerate aldolase + NAD
1llu - PaALDH + NAD + alcohol
4i3v, 4i3w – SmALDH + aldehyde derivative + NAD
4i3x – SmALDH + phosphonoacete + NAD

NADP-dependent ALDH

3k2w - Betaine-ALDH – Pseudoalteromonas atlantica
2hg2, 2opx – Lactaldehyde-EcALDH
2o2p – Formyltetrahydrofolate-rALDH C-terminal
2y51, 2y52, 2y53, 2y5d – BxALDH (mutant) – Burkholderia xenovorans
3ifg, 3ifh - Succinate–semi-ALDH – Burkholderia pseudomallei
3rh9 - Succinate–semi-ALDH – Marinobacter aquaeolei
3uw3 - aspartate–semi-ALDH – Burkholderia thailandensis
3v4c - SmALDH

Binary complexes

2wox, 2wme, 2xdr, 3zqa - Betaine-PaALDH + NADP
3lv1 – Benzaldehyde-PpALDH3 + NADP – Pseudomonas putida
2ilu - Lactaldehyde-EcALDH + NADP
3rhd - Lactaldehyde-MjALDH + NADP - Methanocaldococcus jannaschii
2o2q, 2o2r - Formyltetrahydrofolate-rALDH C-terminal + NADP
3b4w - MtALDH + NADP – Mycobacterium tuberculosis
1eyy, 1ez0 – ALDH + NADP – Vibrio harveyi
3jz4 - Succinate–semi-EcALDH + NADP
3hsk - aspartate–semi-ALDH + NADP – Candida albicans
4h73 - ALDH + NADP – Pyrobaculum

Ternary complexes

3lns - Benzaldehyde-PpALDH3 + NADP + benzoate
2imp - Lactaldehyde-EcALDH + NADH + lactate
2vro – BxALDH + NADP + alcohol


3k9d – ALDH – Listeria monocytogenes

Antiquitin

2jg7 – Antiquitin – Acanthopagrus schlegeli

3my7 – ALDH – Vibrio parahaemolyticus

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.

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