4x0t: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x0t RCSB], [http://www.ebi.ac.uk/pdbsum/4x0t PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4x0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4x0t RCSB], [http://www.ebi.ac.uk/pdbsum/4x0t PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | |||
[[http://www.uniprot.org/uniprot/AL7A1_HUMAN AL7A1_HUMAN]] Pyridoxine-dependent epilepsy. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/AL7A1_HUMAN AL7A1_HUMAN]] Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism.<ref>PMID:16491085</ref> <ref>PMID:20207735</ref> | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 09:50, 1 April 2015
Structure ALDH7A1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+Structure ALDH7A1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+
Structural highlights
Disease[AL7A1_HUMAN] Pyridoxine-dependent epilepsy. The disease is caused by mutations affecting the gene represented in this entry. Function[AL7A1_HUMAN] Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism.[1] [2] Publication Abstract from PubMedThere is growing interest in aldehyde dehydrogenases (ALDHs) because of their overexpression in cancer stem cells and the ability to mediate resistance to cancer drugs. Here, we report the first crystal structure of an aldehyde dehydrogenase complexed with the inhibitor 4-diethylaminobenzaldehyde (DEAB). Contrary to the widely held belief that DEAB is a reversible inhibitor of ALDHs, we show that DEAB irreversibly inactivates ALDH7A1 via formation of a stable, covalent acyl-enzyme species. Diethylaminobenzaldehyde Is a Covalent, Irreversible Inactivator of ALDH7A1.,Luo M, Gates KS, Henzl MT, Tanner JJ ACS Chem Biol. 2015 Jan 6. PMID:25554827[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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