1.1.2.7: methanol dehydrogenase (cytochrome c)
This is an abbreviated version!
For detailed information about methanol dehydrogenase (cytochrome c), go to the full flat file.
Word Map on EC 1.1.2.7
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1.1.2.7
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1.1.99.8
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phenazine
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methylamine
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formaldehyde
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hyphomicrobium
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quinoproteins
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pyrroloquinoline
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methylophilus
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denitrificans
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paracoccus
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methylotrophus
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half-reaction
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linewidth
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quinone-dependent
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methylobacterium
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protiated
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wurster
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methylomonas
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one-electron
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extorquens
- 1.1.2.7
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1.1.99.8
- phenazine
- methylamine
- formaldehyde
- hyphomicrobium
-
quinoproteins
-
pyrroloquinoline
- methylophilus
- denitrificans
-
paracoccus
- methylotrophus
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half-reaction
-
linewidth
-
quinone-dependent
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methylobacterium
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protiated
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wurster
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methylomonas
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one-electron
- extorquens
Reaction
+ 2 ferricytochrome cL = + 2 ferrocytochrome cL + 2 H+
Synonyms
EC 1.1.99.8, Hd-MDH, MDH, MDH2, MEDH, methanol dehydrogenase, More, mxaF, MxaJ, PQQ-dependent methanol dehydrogenase, pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase, QH-ADH, QMDH, quinohemoprotein (type II) alcohol dehydrogenase, quinohemoprotein alcohol dehydrogenase, quinone-dependent alcohol dehydrogenase, quinoprotein alcohol dehydrogenase, quinoprotein dehydrogenase, quinoprotein methanol dehydrogenase, type I MDH, type II MDH
ECTree
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Metals Ions
Metals Ions on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c)
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Ba2+
Ca2+
Fe2+
Na+
binds to cofactor CytcL, binding site analysis
Sr2+
Ca2+ can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+, Sr2+ shows 94% of the activity with Ca2+
can substitute for Ca2+, Ba-MDH has twice the maximum activity of the Ca-MDH but with a much lower affinity for its substrates
Ba2+
Ca2+ can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+, Ba2+ shows 102% of the activity with Ca2+
Ba2+
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modeling of Ba2+-containing MDH active site to investigate the proposed addition-elimination and hydride-transfer methanol oxidation mechanisms. For both mechanisms, almost all the free-energy barriers associated with all of the steps are reduced in the presence of Ba2+-MDH, and they are kinetically feasible. The free energy barriers for methanol oxidation by Ba2+-MDH, particularly for the rate-limiting steps of both mechanisms, are almost half the corresponding barriers calculated for the case of Ca2+-MDH
Diplococcus sp.
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active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
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absolutely required, 1.43 Ca2+ per enzyme tetramer, tightly bound to the active site, preparation of Ca2+-free MDH, which contains a fully-oxidized pyrroloquinoline quinone cofactor, incubation of Ca2+-free MDH with Ca2+ ion leads to reconstituted, fully active enzyme containing fully-reduced, tightly bound PQQ, overview, Ca2+-free enzyme is inactive
Ca2+
binds to cofactor CytcL, binding site analysis
Ca2+
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required for catalytic activity, binding structure, overview
Ca2+
required for activity, functional role analysis, overview
Ca2+
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active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
two Ca2+ ions per enzyme tetramer, essential for the enzymatic activity
Ca2+
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Ca2+ is six-coordinated with bonds to 05, N6, and carboxyl oxygen 07A of PQQ, the two carboxyl oxygen atoms of Glu171, and the side-chain oxygen of Asn255, binding structure, overview
Ca2+
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the active site contains a single Ca2+ whose coordination sphere contains PQQ and protein atoms
Ca2+
bound to the active site, required for catalytic activity
Ca2+
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required, bound at the active site, interaction with the cofactor and the active site residues Arg331, Asp303, and Glu177, but not Asn261, structure overview
Ca2+
binding structure at the active site, overview, the active site contains a single Ca2+ ion whose coordination sphere contains PQQ and protein atoms, including both oxygens of the carboxylate of Glu177 and the amide oxygen of Asn261
Ca2+
one molecule per enzyme alpha-subunit, binding involves Glu177 and Asn261, Ca2+ plays a role in maintaining PQQ in the correct configuration and may also be involved in the catalytic mechanism
Ca2+
required for activity, functional role analysis, overview
Ca2+
the active site contains a single Ca2+ whose coordination sphere contains PQQ and protein atoms
Ca2+
tightly bound close to the inner heme propionate, Ca2+ is involved in stabilization of the redox potential, and is important in the flow of electrons from reduced pyrroloquinoline quinone in methanol dehydrogenase to the heme of cytochrome cL
Ca2+
2 Ca2+ ions are irreversibly incorporated per alpha2beta2 tetramer. Calcium can be replaced in the incorporation process by strontium or barium, the affinities for these ions being similar to that for Ca2+
Ca2+
one molecule of Ca2+ per enzyme tetramer. Ca2+ is directly or indirectly involved in the biding of pyrroloquinoline quinone. Methanol oxidation mutants MoxA-, K- and L- contain no Ca2+. The MoxA, K and L proteins may be involved in maintaining a high Ca2+ concentration in the periplasm. It is more likely, that they fill a chaperone function, stabilizing a configuration of methanol dehydrogenase which permits incorporation of low concentrations of Ca2+ into the protein
Ca2+
one molecule per enzyme alpha-subunit. Neither the quinone form of pyrroloquinoline quinone, nor the disulfide ring or its reduced form are absolutely essential for calcium incorporation into the active site
Ca2+
required for activity, one of the carbonyl oxygens of PQQ is bonded to the Ca2+, probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group
Ca2+
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active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
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active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
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active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
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active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
Ca2+
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active site of QMDH contains one Ca2+ ion, removal of Ca2+ ions results in the loss of the enzyme activity, important role of Ca2+ in the catalysis
in heme c, which is contained in cofactor cytochrome cL, and bound to CytcL, binding sites analysis