Aromatic amine dehydrogenase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:26, 20 March 2019) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
<StructureSection load='2i0s' size='340' side='right' caption='Structure of aromatic amine dehydrogenase with cofactor TTQ complex with phenylacetaldehyde (PDB code [[2i0s]]).' scene=''>
+
<StructureSection load='2i0s' size='350' side='right' caption='Structure of aromatic amine dehydrogenase large subunit (cyan and green) and small subunit (magenta and salmon) with cofactor TTQ complex with phenylacetaldehyde (PDB code [[2i0s]]).' scene='59/593968/Cv/1'>
== Function ==
== Function ==
-
'''Aromatic amine dehydrogenase''' (AADH) catalyzes the conversion of primary aromatic amine and acceptor to aldehyde and reduced acceptor. The acceptor co-factor is tryptophan tryptophylquinone (TTQ).
+
'''Aromatic amine dehydrogenase''' (AADH) catalyzes the conversion of primary aromatic amine and acceptor to aldehyde and reduced acceptor. The acceptor co-factor is tryptophan tryptophylquinone (TTQ).<ref>PMID:8188594</ref>
-
== Disease ==
+
== Structural highlights ==
-
== Relevance ==
+
AADH structure consists of <scene name='59/593968/Cv/2'>2 large</scene> and <scene name='59/593968/Cv/3'>2 small subunits</scene> with the <scene name='59/593968/Cv/5'>co-factor TTQ attached covalently to the small subunit</scene>.<ref>PMID:17475620</ref>
-
 
+
-
== Structural highlights ==
+
==3D structures of aromatic amine dehydrogenase==
==3D structures of aromatic amine dehydrogenase==
 +
[[Aromatic amine dehydrogenase 3D structures]]
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
</StructureSection>
-
 
+
-
[[2ah1]] – AfAADH – ''Alcaligenes faecalis''<br />
+
-
[[2i0r]], [[2iup]], [[2iur]], [[2iuv]], [[2iot]], [[2oiz]] – AfAADH + TTQ derivative<br />
+
-
[[2agl]] – AfAADH + TTQ derivative + phenylhydrazine <br />
+
-
[[2agw]], [[2iuq]] – AfAADH + TTQ derivative + tryptamine<br />
+
-
[[2agx]], [[2agy]] – AfAADH + TTQ derivative + indol ethanimine<br />
+
-
[[2ojy]] – AfAADH + TTQ derivative + indol acetamide<br />
+
-
[[2agz]], [[2ah0]] – AfAADH + TTQ derivative + indol aminoethanol<br />
+
-
[[2ok6]] – AfAADH + TTQ derivative + formyl amino tryptophan<br />
+
-
[[2hxc]] – AfAADH + TTQ + benzylamine<br />
+
-
[[2hj4]], [[2hjb]] – AfAADH + TTQ derivative + benzylamine derivative<br />
+
-
[[2i0s]] – AfAADH + TTQ + phenylacetaldehyde<br />
+
-
[[2ok4]] – AfAADH + TTQ derivative + phenylacetaldehyde<br />
+
-
[[2q7q]] – AfAADH + TTQ derivative + phenyl methanamine<br />
+
-
[[2hkm]] – AfAADH + TTQ derivative + phenyl ethyl amine<br />
+
-
[[2hkr]] – AfAADH + TTQ derivative + methoxyphenyl ethanamide + methoxyphenyl acetamide<br />
+
-
[[2h3x]], [[2h47]], [[2iaa]] – AfAADH + TTQ derivative + azurin<br />
+
-
 
+
== References ==
== References ==

Current revision

Structure of aromatic amine dehydrogenase large subunit (cyan and green) and small subunit (magenta and salmon) with cofactor TTQ complex with phenylacetaldehyde (PDB code 2i0s).

Drag the structure with the mouse to rotate

References

  1. Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL, Edwards SL. Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J Bacteriol. 1994 May;176(10):2922-9. PMID:8188594
  2. Roujeinikova A, Hothi P, Masgrau L, Sutcliffe MJ, Scrutton NS, Leys D. New insights into the reductive half-reaction mechanism of aromatic amine dehydrogenase revealed by reaction with carbinolamine substrates. J Biol Chem. 2007 Aug 17;282(33):23766-77. Epub 2007 May 1. PMID:17475620 doi:10.1074/jbc.M700677200

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel

Personal tools