2q7q
From Proteopedia
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|PDB= 2q7q |SIZE=350|CAPTION= <scene name='initialview01'>2q7q</scene>, resolution 1.600Å | |PDB= 2q7q |SIZE=350|CAPTION= <scene name='initialview01'>2q7q</scene>, resolution 1.600Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=C2B:1-(4-CHLOROPHENYL)METHANAMINE'>C2B</scene> | + | |LIGAND= <scene name='pdbligand=C2B:1-(4-CHLOROPHENYL)METHANAMINE'>C2B</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase Aralkylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.4 1.4.99.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase Aralkylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.4 1.4.99.4] </span> |
|GENE= aauA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 Alcaligenes faecalis]), aauB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 Alcaligenes faecalis]) | |GENE= aauA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 Alcaligenes faecalis]), aauB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 Alcaligenes faecalis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q7q OCA], [http://www.ebi.ac.uk/pdbsum/2q7q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q7q RCSB]</span> | ||
}} | }} | ||
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[[Category: Leys, D.]] | [[Category: Leys, D.]] | ||
[[Category: Roujeinikova, A.]] | [[Category: Roujeinikova, A.]] | ||
| - | [[Category: C2B]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: ttq]] | [[Category: ttq]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:45:56 2008'' |
Revision as of 01:45, 31 March 2008
| |||||||
| , resolution 1.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | aauA (Alcaligenes faecalis), aauB (Alcaligenes faecalis) | ||||||
| Activity: | Aralkylamine dehydrogenase, with EC number 1.4.99.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Alcaligenes faecalis AADH in complex with p-chlorobenzylamine.
Overview
Structure-activity correlations have been employed previously in the mechanistic interpretation of TTQ-dependent amine dehydrogenases using a series of para-substituted benzylamines. However, by combining the use of kinetic isotope effects (KIEs) and crystallographic analysis, in conjunction with structure-reactivity correlation studies, we show that para-substituted benzylamines are poor reactivity probes for TTQ-dependent aromatic amine dehydrogenase (AADH). Stopped-flow kinetic studies of the reductive half-reaction, with para-substituted benzylamines and their dideuterated counterparts, demonstrate that C-H or C-D bond breakage is not fully rate limiting (KIEs approximately unity). Contrary to previous reports, Hammett plots exhibit a poor correlation of structure-reactivity data with electronic substituent effects for para-substituted benzylamines and phenylethylamines. Crystallographic studies of enzyme-substrate complexes reveal that the observed structure-reactivity correlations are not attributed to distinct binding modes for para-substituted benzylamines in the active site, although two binding sites for p-nitrobenzylamine are identified. We identify structural rearrangements, prior to the H-transfer step, which are likely to limit the rate of TTQ reduction by benzylamines. This work emphasizes (i) the need for caution when applying structure-activity correlations to enzyme-catalyzed reactions and (ii) the added benefit of using both isotope effects and structural analysis, in conjunction with structure-reactivity relationships, to study chemical steps in enzyme reaction cycles.
About this Structure
2Q7Q is a Protein complex structure of sequences from Alcaligenes faecalis. Full crystallographic information is available from OCA.
Reference
Isotope effects reveal that para-substituted benzylamines are poor reactivity probes of the quinoprotein mechanism for aromatic amine dehydrogenase., Hothi P, Roujeinikova A, Khadra KA, Lee M, Cullis P, Leys D, Scrutton NS, Biochemistry. 2007 Aug 14;46(32):9250-9. Epub 2007 Jul 18. PMID:17636875
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