Methylamine dehydrogenase

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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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[[1mda]], [[2j55]], [[2j56]], [[2j57]], [[3c75]] – PdMADH α + β + amicyanin – ''Paracoccus denitrificans''<br />
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*Methylamine dehydrogenase
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[[1mae]], [[1maf]], [[2bbk]], [[2mad]] – PdMADH α + β<br />
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[[2mta]], [[2gc7]] - PdMADH α + β + amicyanin + cytochrome c551i<br />
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[[1mg2]], [[1mg3]], [[2gc4]] - PdMADH α (mutant) + β+ amicyanin + cytochrome c551i<br />
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[[3rn1]], [[3sle]], [[3svw]], [[3sws]], [[3sxt]], [[4k3i]] - PdMADH α + β + MauG<br />
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[[3sjl]] - PdMADH α + β (mutant) + MauG<br />
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===pre-MADH===
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**[[1mda]], [[2j55]], [[2j56]], [[2j57]], [[3c75]] – PdMADH α + β + amicyanin – ''Paracoccus denitrificans''<br />
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**[[1mae]], [[1maf]], [[2bbk]], [[2mad]] – PdMADH α + β<br />
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**[[2mta]], [[2gc7]] - PdMADH α + β + amicyanin + cytochrome c551i<br />
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**[[1mg2]], [[1mg3]], [[2gc4]] - PdMADH α (mutant) + β+ amicyanin + cytochrome c551i<br />
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**[[3rn1]], [[3sle]], [[3svw]], [[3sws]], [[3sxt]], [[4k3i]] - PdMADH α + β + MauG<br />
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**[[3sjl]] - PdMADH α + β (mutant) + MauG<br />
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[[3l4m]], [[3l4o]] - PdMADH α + β (mutant) + MauG<br />
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*pre-MADH
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[[3orv]] - PdMADH α + β (mutant) + MauG (mutant)<br />
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[[3pxs]], [[4fa1]], [[4fa4]], [[4fa5]], [[4fa9]], [[4fan]], [[4fav]], [[4fb1]] - PdMADH α + β + MauG<br />
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[[3pxt]] - PdMADH α + β + CO + MauG<br />
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[[3pxw]] - PdMADH α + β + NO + MauG<br />
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[[3rlm]], [[3rmz]], [[3rn0]], [[4l1q]], [[4l3g]], [[4l3h]] - PdMADH α + β + MauG (mutant)
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**[[3l4m]], [[3l4o]] - PdMADH α + β (mutant) + MauG<br />
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**[[3orv]] - PdMADH α + β (mutant) + MauG (mutant)<br />
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**[[3pxs]], [[4fa1]], [[4fa4]], [[4fa5]], [[4fa9]], [[4fan]], [[4fav]], [[4fb1]] - PdMADH α + β + MauG<br />
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**[[3pxt]] - PdMADH α + β + CO + MauG<br />
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**[[3pxw]] - PdMADH α + β + NO + MauG<br />
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**[[3rlm]], [[3rmz]], [[3rn0]], [[4l1q]], [[4l3g]], [[4l3h]] - PdMADH α + β + MauG (mutant)
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}}
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:26, 1 December 2014

Template:STRUCTURE 2j55 Methylamine dehydrogenase (MADH) catalyzes the oxidative deamination of primary amine to aldehyde and ammonia, in particular, the conversion of methylamine to formaldehyde. MADH is tryptophan tryptophyl-quinone (TTQ) dependent. MADH is a heterotetramer containing heavy (α) and light (β) subunits. Each β subunit contains a TTQ prosthetic group. The posttranslational modification of two tryptophan residues to form the TTQ cofactor of MADH is catalyzed by methylation utilization protein (MauG). MADH forms a complex with cytochrome c-551i. In the complex, electrons are transferred from TTQ via the amicyanin copper ion center to the heme group of cytochrome.

3D structures of methylamine dehydrogenase

Updated on 01-December-2014

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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