Methanol dehydrogenase
From Proteopedia
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | <StructureSection load=' | + | <StructureSection load='' size='350' side='right' scene='49/490936/Cv/1' caption='Methanol dehydrogenase large subunit (cyan and deeppink) and small subunit (green and yellow) complex with cofactor PQQ and Ca+2 ion (green), [[2ad6]]'> |
== Function == | == Function == | ||
| - | '''Methanol dehydrogenase''' (MDH) is a quinoprotein which catalyzes the conversion of methanol and NAD+ or NADP+ to formaldeyde and NADH or NADPH and H+. MDH is a pyrroloquinoline quinone (PQQ)-dependent enzyme. MDH requires a divalent cation like Ca+2 for catalytic activity<ref>PMID:12686102</ref>. | + | '''Methanol dehydrogenase''' or '''sulfoacetaldehyde reductase''' (MDH) is a quinoprotein which catalyzes the conversion of methanol and NAD+ or NADP+ to formaldeyde and NADH or NADPH and H+. MDH is a pyrroloquinoline quinone (PQQ)-dependent enzyme. MDH requires a divalent cation like Ca+2 for catalytic activity<ref>PMID:12686102</ref>. |
== Structural highlights == | == Structural highlights == | ||
| - | <scene name='49/490936/Cv/ | + | <scene name='49/490936/Cv/6'>PQQ and the hexa-coordinated Ca+2</scene> are bound in a <scene name='49/490936/Cv/7'>funnel-shaped internal cavity of MDH</scene><ref>PMID:21356200</ref>. Water molecules are shown as red spheres. |
</StructureSection> | </StructureSection> | ||
==3D structures of methanol dehydrogenase== | ==3D structures of methanol dehydrogenase== | ||
| Line 17: | Line 17: | ||
[[1lrw]] - MDH α+β + Ca + PQQ – ''Paracoccus denitrificans''<br /> | [[1lrw]] - MDH α+β + Ca + PQQ – ''Paracoccus denitrificans''<br /> | ||
[[2d0v]] - MDH α+β + Ca + PQQ – ''Hyphomicrobium denitrificans''<br /> | [[2d0v]] - MDH α+β + Ca + PQQ – ''Hyphomicrobium denitrificans''<br /> | ||
| - | [[4mae]] - | + | [[4mae]] - MfMDH + Ce + PQQ – ''Methylacidiphilum fumariolicum''<br /> |
| - | [[ | + | [[6fkw]] - MfMDH + Eu + PQQ <br /> |
| + | [[7ced]] - McMDH α+β – ''Methylococcus capsulatus''<br /> | ||
| + | [[4tqo]], [[7cdl]], [[7ce5]], [[7ce9]], [[7cfx]] - McMDH α+β + Ca + PQQ <br /> | ||
| + | [[5xm3]] - MDH α+β + Mg + PQQ – ''Methylophaga aminisulfidivorans''<br /> | ||
| + | [[6dam]] - MDH + La + PQQ – ''Methyomicrobium byryatense''<br /> | ||
| + | [[6jko]] - BkMDH + Zn – ''Bifidobacterium kashiwanohense''<br /> | ||
| + | [[6jkp]] - BkMDH + Zn + NAD<br /> | ||
| + | [[6onp]], [[6onq]] - MexMDH – ''Methylorubrum extorquens''<br /> | ||
| + | [[6oc5]] - MexMDH + La <br /> | ||
| + | [[6oc6]] - MexMDH + La + PQQ<br /> | ||
| + | [[7o6z]] - MDH α + Nd + PQQ – ''Methylacidimicrobium''<br /> | ||
| + | |||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
| |||||||||||
3D structures of methanol dehydrogenase
Updated on 02-November-2021
4aah, 1g72, 2ad6, 2ad7, 2ad8 – MmMDH α+β + Ca + PQQ – Methylophilus methylotrophus
1h4i, 1w6s - MeMDH α+β + Ca + PQQ – Methylobacterium extorquens
1h4j - MeMDH α (mutant) +β + Ca + PQQ
1lrw - MDH α+β + Ca + PQQ – Paracoccus denitrificans
2d0v - MDH α+β + Ca + PQQ – Hyphomicrobium denitrificans
4mae - MfMDH + Ce + PQQ – Methylacidiphilum fumariolicum
6fkw - MfMDH + Eu + PQQ
7ced - McMDH α+β – Methylococcus capsulatus
4tqo, 7cdl, 7ce5, 7ce9, 7cfx - McMDH α+β + Ca + PQQ
5xm3 - MDH α+β + Mg + PQQ – Methylophaga aminisulfidivorans
6dam - MDH + La + PQQ – Methyomicrobium byryatense
6jko - BkMDH + Zn – Bifidobacterium kashiwanohense
6jkp - BkMDH + Zn + NAD
6onp, 6onq - MexMDH – Methylorubrum extorquens
6oc5 - MexMDH + La
6oc6 - MexMDH + La + PQQ
7o6z - MDH α + Nd + PQQ – Methylacidimicrobium
References
- ↑ Anthony C, Williams P. The structure and mechanism of methanol dehydrogenase. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):18-23. PMID:12686102
- ↑ Li J, Gan JH, Mathews FS, Xia ZX. The enzymatic reaction-induced configuration change of the prosthetic group PQQ of methanol dehydrogenase. Biochem Biophys Res Commun. 2011 Mar 25;406(4):621-6. Epub 2011 Feb 26. PMID:21356200 doi:10.1016/j.bbrc.2011.02.107
