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
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quinoproteins
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pyrroloquinoline
- methylophilus
- denitrificans
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paracoccus
- 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
- 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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Subunits
Subunits on EC 1.1.2.7 - methanol dehydrogenase (cytochrome c)
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dimer
heterotetramer
monomer
pentamer
tetramer
additional information
x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
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Methylorubrum extorquens ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
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x * 62000, alpha-subunit, + x * 7500, beta-subunit, SDS-PAGE
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alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits
heterotetramer
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alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits
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heterotetramer
alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits
heterotetramer
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alpha2beta2, the MEDH heterotetramer is composed of two large subunits and two small subunits
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1 * 18000, cytochrome cL, SDS-PAGE
monomer
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in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methyloversatilis universalis strain FAM5 is a monosubunit protein
monomer
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in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methyloversatilis universalis strain FAM5 is a monosubunit protein
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2 * 65980, subunit alpha, + 2 * 7580, subunit beta, + 1 * 27860, MxaJ protein, type II MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer, and contains an additional MxaJ protein
pentamer
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2 * 65980, subunit alpha, + 2 * 7580, subunit beta, + 1 * 27860, MxaJ protein, type II MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer, and contains an additional MxaJ protein
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2 * 65000, alpha-subunit, + 2 * 9000, beta-subunit, SDS-PAGE
tetramer
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alpha2beta2 structure, subunit organization and structure, docking model, overview
tetramer
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alpha2beta2 structure, subunit organization and structure, docking model, overview
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tetramer
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2 * 65000, alpha-subunit, + 2 * 9000, beta-subunit, SDS-PAGE
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tetramer
2 * 65980, subunit alpha, + 2 * 7580, subunit beta, type I MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer
tetramer
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2 * 65980, subunit alpha, + 2 * 7580, subunit beta, type I MDH consists of two identical dimers of alpha and beta subunits organized to form the alpha2beta2 tetramer
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tetramer
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2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination
tetramer
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2 * 62000, alpha-subunit, + 2 * 8000, beta-subunit, alpha2beta2-structure, crystal structure determination
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tetramer
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alpha2beta2 subunit conposition, structure model of an alphabeta unit from crystal structure determination, overview
tetramer
2 * 66000 + 2 * 8500, alpha2beta2, crystal structure determination
tetramer
alpha2beta2, comparison of wild-type and mutant enzyme structures, overview
tetramer
alpha2beta2, the alpha-subunit has an 8fold radial symmetry, with its eight 3-sheets stabilized by a novel tryptophan docking motif. The PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulfide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond, subunit structures and interactions, overview
tetramer
alpha2beta2, three-dimensional structure, modelling, overview
tetramer
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alpha2beta2, comparison of wild-type and mutant enzyme structures, overview
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Diplococcus sp.
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the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
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in contrast to other two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenases, wide-spread in Burkholderiales, the enzyme from Methylibium petroleiphilum strain PM1 is a monosubunit protein
additional information
the alpha-subunit is known to function as the active site for the oxidoreduction reaction, which includes the PQQ group as a redox cofactor and a calcium ion coordinated to vicinal charged and hydrophobic amino-acid residues
additional information
the original conformation of the MDH Methylophaga aminisulfidivorans MPT is most likely the alpha2beta2-MxaJ complex
additional information
the original conformation of the MDH Methylophaga aminisulfidivorans MPT is most likely the alpha2beta2-MxaJ complex
additional information
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the original conformation of the MDH Methylophaga aminisulfidivorans MPT is most likely the alpha2beta2-MxaJ complex
additional information
the MxaJ molecule consists of nine alpha-helices (alpha1-alpha9) and six beta-strands (beta1-beta6), which are partitioned to form two globular domains (domain-1 and 2). The two domains are connected by a long and rigid beta-strand (beta3) at the center, and each domain has a different arrangement of alpha/beta secondary structural element. Detailed MxaJ structure analysis, overview
additional information
the overall interaction between beta-subunits and alpha-subunits of Ma-MDH is stronger than that of terrestrial homologues, providing the structural integrity to Ma-MDH in aquatic environments
additional information
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the MxaJ molecule consists of nine alpha-helices (alpha1-alpha9) and six beta-strands (beta1-beta6), which are partitioned to form two globular domains (domain-1 and 2). The two domains are connected by a long and rigid beta-strand (beta3) at the center, and each domain has a different arrangement of alpha/beta secondary structural element. Detailed MxaJ structure analysis, overview
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additional information
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the overall interaction between beta-subunits and alpha-subunits of Ma-MDH is stronger than that of terrestrial homologues, providing the structural integrity to Ma-MDH in aquatic environments
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additional information
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the original conformation of the MDH Methylophaga aminisulfidivorans MPT is most likely the alpha2beta2-MxaJ complex
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additional information
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the alpha-subunit is known to function as the active site for the oxidoreduction reaction, which includes the PQQ group as a redox cofactor and a calcium ion coordinated to vicinal charged and hydrophobic amino-acid residues
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additional information
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the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
three-dimensional structrue determination of MEDH with bound methanol or ethanol, overview
additional information
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the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
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additional information
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three-dimensional structrue determination of MEDH with bound methanol or ethanol, overview
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additional information
the large alpha-subunit has a propeller fold making up a superbarrel of eight radially arranged beta-sheets, i.e. the propeller blades, containing the tryptophan-docking motifs that link together the eight beta-sheets, and the presence in the active site of a unique eight-membered disulfide ring structure formed from adjacent cysteine residues 103 and 104, joined by an atypical non-planar peptide bond
additional information
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the periplasmic protein contains both a PQQ-containing domain, folded into a beta-propeller fold, and a smaller cytochrome c domain, which is analogous to a typical class I c-type cytochrome, these two domains are connected via a proline-rich linker region, which lacks any secondary structure, structure model of the electron-transfer complex formed by MDH and cytochrome cL, overview
additional information
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the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
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the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
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the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
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the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5
additional information
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the enzyme shows a propeller structure, QMDH contains a disulfide structure that is similar to the analogous structure in QEDH, EC 1.1.5.5